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Selective Covalent Modification of Membrane Components

  • Chapter
The Enzymes of Biological Membranes

Abstract

Essential to an understanding of membrane-related biological phenomena at the molecular level is not only identification of the components involved but rather knowledge of their respective structural and functional characteristics. Such knowledge is attained by disintegrating biological membranes into particulate entities whose chemical properties can then be more specifically investigated. Successful reconstitution of isolated components in model systems leads to an improved understanding of transmembrane processes. Membrane architecture and the mechanism of transbilayer events are, however, most conclusively explored within a functionally active membrane. The latter approach therefore requires selective identification of defined membrane components in situ. As a consequence, the search for means to locate and specifically characterize defined membrane constituents has intentionally been pursued. This objective is most efficiently achieved by the use of chemical modification. In spite of inherent limitations, the approach offers obvious advantages in that (1) the extent and topology of label binding can be controlled chemically, and (2) label allocation is feasible at both the membrane and molecular level.

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References

  • Abbott, R. E., and Schachter, D., 1976, Impermeant maleimides, J. Biol. Chem. 251:7176–7183.

    PubMed  CAS  Google Scholar 

  • Abu-Salah, K. M., and Findlay, J. B. L., 1977, Labeling of egg phosphatidylcholine vesicles and myeline membrane with a photoreactive lipophilic reagent, Biochem. J. 161:223–228.

    PubMed  CAS  Google Scholar 

  • Allegrini, P. R., Sigrist, H., Schaller, J., and Zahler, P., 1983, Site-directed fluorogenic modification of bacteriorhodopsin by 7-chloro-4-nitrobenz-2oxa-1,3-diazole, Eur. J. Biochem. 132:603–608.

    Article  PubMed  CAS  Google Scholar 

  • Andersen, H. C., 1978, Probes of membrane structure, Annu. Rev. Biochem. 47:359–383.

    Article  PubMed  CAS  Google Scholar 

  • Andersen, J. P., and Møller, J. V., 1977, Reaction of sarcoplasmic reticulum Ca2+-ATPase in different functional states with 5,5′-dithiobis(2-nitrobenzoate), Biochim. Biophys. Acta 485:188–202.

    Article  PubMed  CAS  Google Scholar 

  • Anderson, G. W., Zimmermann, J. E., and Callahan, F. M., 1964, The use of esters of N-hydroxysuccinimide in peptide synthesis, J. Am. Chem. Soc. 86:1839–1842.

    Article  CAS  Google Scholar 

  • Barzilay, M., Ship, S., and Cabantchik, Z. I., 1979, Anion transport in red blood cells. I. Chemical properties of anion recognition sites as revealed by structure-activity relationships of aromatic sulfonic acids, Membr. Biochem. 2:227–254.

    Article  PubMed  CAS  Google Scholar 

  • Bayley, H., 1982, Photoactivated hydrophobic reagents for integral membrane proteins, in: Membranes and Transport, Vol. 1 (A. N. Martonosi, ed.), Plenum Press, New York, pp. 185–194.

    Chapter  Google Scholar 

  • Bayley, H., and Knowles, J. R., 1978a, Photogenerated reagents for membrane labeling. 1. Phenylnitrene formed within the lipid bilayer, Biochemistry 17:2414–2419.

    Article  PubMed  CAS  Google Scholar 

  • Bayley, H., and Knowles, J. R., 1978b, Photogenerated reagents for membrane labeling. 2. Phenylcarbene and adamantylidene formed within the lipid bilayer, Biochemistry 17:2420–2423.

    Article  PubMed  CAS  Google Scholar 

  • Bayley, H., and Knowles, J. R., 1980, Photogenerated reagents for membranes: Selective labeling of intrinsic membrane proteins in the human erythrocyte membrane, Biochemistry 19:3883–3892.

    Article  PubMed  CAS  Google Scholar 

  • Bayley, H., Huang, K. S., Radhakrishnan, R., Ross, A. H., Takagaki, J., and Khorana, H. G., 1981, Site of attachment of retinal in bacteriorhodopsin, Proc. Natl. Acad. Sci. USA 78:2225–2229.

    Article  PubMed  CAS  Google Scholar 

  • Bercovici, T., and Gitler, C., 1978, 5-[125I]Iodonaphtyl azide, a reagent to determine the penetration of proteins into the lipid bilayer of biological membranes, Biochemistry 17:1484–1489.

    Article  PubMed  CAS  Google Scholar 

  • Bijlenga, R. K. L., Briottet, C., and Jaton, J. C., 1982, Structural differences between heavy chains of secreted and membrane-bound IGM of a human lymphoblastoid cell line, Mol. Immunol. 19:45–49.

    Article  PubMed  CAS  Google Scholar 

  • Birkett, D. J., Price, N. C., Radda, G. K., and Salmon, A. G., 1970, The reactivity oi SH groups with a fluorogenic reagent, FEBS Lett. 6:346–348.

    Article  PubMed  CAS  Google Scholar 

  • Bishop, D. G., Op den Kamp, J. A. F., and Van Deenen, L. L. M., 1977, The distribution of lipids in the protoplast membranes of Bacillus subtilis, Eur. J. Biochem. 80:381–391.

    Article  PubMed  CAS  Google Scholar 

  • Bishop, D. G., Bevers, E. M., van Meer, G., Op den Kamp, J. A. F., and Van Deenen, L. L. M., 1979, A monolayer study of the reaction of trinitrobenzene sulfonic acid with amino phospholipids, Biochim. Biophys. Acta 551:122–128.

    Article  PubMed  CAS  Google Scholar 

  • Bisson, R., and Montecucco, C., 1981, Photolabelling of membrane proteins with photoactive phospholipids, Biochem. J. 193:757–763.

    PubMed  CAS  Google Scholar 

  • Bisson, R., Montecucco, C., Gutweniger, H., and Azzi, A., 1979, Cytochrome c oxidase subunits in contact with phospholipids, J. Biol. Chem. 254:9962–9965.

    PubMed  CAS  Google Scholar 

  • Boulay, F., Lauquin, G. J. M., Tsugita, A., and Vignais, P. V., 1983, Photolabeling approach to the study of the topography of the atractyloside binding site in mitochondrial adenosine 5′-diphosphate/adenosine 5′-triphosphate carrier protein, Biochemistry 22:277–484.

    Article  Google Scholar 

  • Bretscher, M. S., 1972, Phosphatidyl-ethanolamine: Differential labelling in intact cells and cell ghosts of human erythrocytes by a membrane-impermeable reagent, J. Mol. Biol. 71:523–528.

    Article  PubMed  CAS  Google Scholar 

  • Bruice, T. C., Gregory, J. J., and Walters, S. L., 1968, Reactions of tetranitromethane. I. Kinetics and mechanism of nitration of phenols by tetranitromethane, J. Am. Chem. Soc. 90:1612–1619.

    Article  CAS  Google Scholar 

  • Brunner, J., 1981, Labelling the hydrophobic core of membranes, TIBS 6:44–46.

    CAS  Google Scholar 

  • Brunner, J., and Richards, F. M., 1980, Analysis of membranes photolabeled with lipid analogues, J. Biol. Chem. 255:3319–3329.

    PubMed  CAS  Google Scholar 

  • Brunner, J., and Semenza, G., 1981, Selective labeling of the hydrophobic core of membranes with 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine, a carbene-generating reagent, Biochemistry 20: 7174–7182.

    Article  PubMed  CAS  Google Scholar 

  • Bunnett, J. F., 1963, Nucleophilic reactivity, Annu. Rev. Phys. Chem. 14:271–290.

    Article  CAS  Google Scholar 

  • Cabantchik, Z. I., and Rothstein, A., 1974, Membrane proteins related to anion permeability of human red cells. I. Localization of disulfonic stilbene binding sites in proteins involved in permeation, J. Membr. Biol. 15:207–266.

    Article  PubMed  CAS  Google Scholar 

  • Cabantchik, Z. I., Knauf, P. A., and Rothstein, A., 1978, The anion transport system of the red blood cell: The role of membrane protein evaluated by the use of “probes,” Biochim. Biophys. Acta 515:239–302.

    Article  PubMed  CAS  Google Scholar 

  • Campos-Cavieres, M., Moore, T. A., and Perham, R. N., 1979, Effects of modification of the tyrosine residues of bacteriorhodopsin with tetranitromethane, Biochem. J. 179:233–238.

    PubMed  CAS  Google Scholar 

  • Capaldi, R. A., Briggs, M. M., and Smith, R. J., 1979, Cleavable bifunctional reagents for studying near neighbour relationships among mitochondrial inner membrane complexes, Meth. Enzymol. 56:630–642.

    Article  PubMed  CAS  Google Scholar 

  • Carey, P. R., and Schneider, H., 1978, Resonance Raman labels: A submolecular probe for interactions in biochemical and biological systems, Acc. Chem. Res. 11:122–128.

    Article  CAS  Google Scholar 

  • Carraway, K., 1975, Covalent labeling of membranes, Biochim. Biophys. Acta 415:379–410.

    Article  PubMed  Google Scholar 

  • Cerletti, N., and Schatz, G., 1979, Cytochrome c oxidase from bakers’ yeast: Photolabeling of subunits exposed to the lipid bilayer, J. Biol. Chem. 254:7746–7751.

    PubMed  CAS  Google Scholar 

  • Chakrabarti, P., and Khorana, H. G., 1975, A new approach to the study of phospholipid-protein interactions in biological membranes. Synthesis of fatty acids and phospholipids containing photosensitive groups, Biochemistry 14:5021–5033.

    Article  PubMed  CAS  Google Scholar 

  • Chapman, D., Gomez-Fernandez, J. C., and Goñi, F. M., 1982, The interaction of intrinsic proteins and lipids in biomembranes, TIBS 7:67–70.

    CAS  Google Scholar 

  • Chowdhry, V., and Westheimer, F. H., 1979, Photoaffinity labeling of biological systems, Annu. Rev. Biochem. 48:293–325.

    Article  PubMed  CAS  Google Scholar 

  • Cuatrecasas, P., and Parikh, I., 1972, Adsorbents for affinity chromatography. Use of N-hydroxysuccinimide esters of agarose, Biochemistry 11:2291–2299.

    Article  PubMed  CAS  Google Scholar 

  • Czarnecki, J. J., Abbott, M. S., and Selman, B. R., 1982, Photoaffinity labeling with 2-azidoadenosine diphosphate of a tight nucleotide binding site on chloroplast coupling factor 1, Proc. Natl. Acad. Sci. USA 79:7744–7748.

    Article  PubMed  CAS  Google Scholar 

  • Das, M., and Fox, C. F., 1979, Chemical cross-linking in biology, Annu. Rev. Biophys. Bioeng. 8:165–193.

    Article  PubMed  CAS  Google Scholar 

  • Dellweg, H. G., and Sumper, M., 1978, Selective formation of bacterio-opsin trimers by chemical cross-linking of purple membrane, FEBS Lett. 90:123–126.

    Article  PubMed  CAS  Google Scholar 

  • Deters, D. W., Racker, E., Nelson, N., and Nelson, H., 1975, Partial resolution of the enzymes catalyzing photophosphorylation. XV. Approaches to the active site of coupling factor 1, J. Biol. Chem. 250:1041–1047.

    PubMed  CAS  Google Scholar 

  • Drobnica, L., Kristian, P., and Augustin, J., 1977, The Chemistry of the-NCS group, in: The Chemistry of Cyanates and Their Thioderivatives, Part 2 (S. Patai, ed.), Wiley, New York, pp. 1002–1222.

    Google Scholar 

  • Edwards, R. M., Kempson, S. A., Carlson, G. L., and Dousa, T. P., 1979, Diazotized [125I]diiodosulfanilic acid as a label for cell surface membranes, Biochim. Biophys. Acta 553:54–65.

    Article  PubMed  CAS  Google Scholar 

  • Engelman, D. M., Henderson, R., McLachan, A. D., and Wallace, B. A., 1980, Path of the Polypeptide in bacteriorhodopsin, Proc. Natl. Acad. Sci. USA 77:2023–2027.

    Article  PubMed  CAS  Google Scholar 

  • Esch, F. S., Böhlen, P., Otsuka, A. S., Yoshida, M., and Allison, W. S., 1981, Inactivation of the bovine mitochondrial F1-ATPase with dicyclohexyl[14C]carbodiimide leads to the modification of a specific glutamic acid residue in the β-subunit, J. Biol. Chem. 256:9084–9089.

    PubMed  CAS  Google Scholar 

  • Fager, R. S., Kutina, C. B., and Abrahamson, E. W., 1973, The use of NBD chloride (7-chloro-4-nitrobenzo-2-oxa-1,3-diazole) in detecting amino acids and as N-terminal reagent, Anal. Biochem. 53:290–294.

    Article  PubMed  CAS  Google Scholar 

  • Fannin, E. F., Evans, J. O., Gibbs, E. M., and Diedrich, D. F., 1981, Phloretinyl-3′-benzylazide: A high affinity probe for the sugar transporter in human erythrocytes. 1. Hexose transport inhibition and photolabeling of mutarotase, Biochim. Biophys. Acta 649:189–201.

    Article  PubMed  CAS  Google Scholar 

  • Farley, R. A., Goldman, D. W., and Bayley, H., 1980, Identification of regions of the catalytic subunit of (Na — K)-ATPase embedded within the cell membrane, J. Biol. Chem. 38:234–236.

    Google Scholar 

  • Ferguson, S. J., Lloyd, W. J., Lyons, M. H., and Radda, G. K., 1975, The mitochondrial ATPase. Evidence for a single essential tyrosine residue, Eur. J. Biochem. 54:117–126.

    Article  PubMed  CAS  Google Scholar 

  • Fonda, M. L., and Anderson, B. M., 1969, D-Amino acid oxidase. IV. Inactivation by maleimides, J. Biol. Chem. 244:666–674.

    PubMed  CAS  Google Scholar 

  • Freedman, R. B., 1979, Cross-linking reagents and membrane organization, TIBS 4:193–197.

    CAS  Google Scholar 

  • Freedman, R. B., and Radda, G. K., 1968, The reaction of 2,4,6,-trinitrobenzenesulfonic acid with amino acids, peptides and proteins, Biochem. J. 108:383–391.

    PubMed  CAS  Google Scholar 

  • Frei, E., and Zahler, P., 1979, Phospholipase A2 from sheep erythrocyte membranes: Ca2+ dependence and localization, Biochim. Biophys. Acta 550:450–463.

    Article  PubMed  CAS  Google Scholar 

  • Frielle, T., Brunner, J., and Curthoys, N. P., 1982, Isolation of the hydrophobic membrane binding domain of rat renal γ-glutamyl transpeptidase selectively labeled with 3-trifluoromethyl-3-(m[125I]-iodophenyl)diazirine, J. Biol. Chem. 257:14979–14982.

    PubMed  CAS  Google Scholar 

  • Furthmayr, H., Galardy, R. E., Tomita, M., and Marchesi, V. T., 1978, The intramembranous segment of human erythrocyte glycophorin A, Arch. Biochem. Biophys. 185:21–29.

    Article  PubMed  CAS  Google Scholar 

  • Gahmberg, C. G., 1981, Membrane glycoproteins and glycolipids: Structure, localization and function of the carbohydrate, in: Membrane Structure, Vol. 1 (J. B. Finean and R. H. Michell, eds.), Elsevier/North-Holland Biomedical Press, Amsterdam, pp. 127–160.

    Chapter  Google Scholar 

  • Gahmberg, C. G., and Andersson, L. C., 1977, Selective radioactive labeling of cell surface sialoglyco-proteins by periodate-tritiated borohydride, J. Biol. Chem. 252:5888–5894.

    PubMed  CAS  Google Scholar 

  • Gahmberg, C. G., and Hakomori, S., 1973, External labeling of cell surface galactose and galactosamine in glycolipid and glycoprotein of human erythrocytes, J. Biol. Chem. 248:4311–4317.

    PubMed  CAS  Google Scholar 

  • Gerber, G. E., and Khorana, H. G., 1982, Primary structure of bacteriorhodopsin: Sequencing methods for membrane proteins, Meth. Enzymol. 88:56–74.

    Article  CAS  Google Scholar 

  • Gitler, C., and Bercovici, T., 1980, Use of lipophilic photoactivatable reagents to identify the lipid embedded domains of membrane proteins, Ann. N.Y. Acad. Sci. 346:199–211.

    Article  PubMed  CAS  Google Scholar 

  • Glazer, A. N., 1976, The chemical modification of proteins by group-specific and site-specific reagents, in: The Proteins, Vol. 1 (N. Neurath and R. L. Hill, eds.), Academic Press, London, pp. 1–103.

    Google Scholar 

  • Gordesky, S. E., Marinetti, G. V., and Love, R., 1975, The reaction of chemical probes with the erythrocyte membrane, J. Membr. Biol. 20:111–132.

    Article  PubMed  CAS  Google Scholar 

  • Gupta, C. M., Radhakrishnan, R., Gerber, G. E., Olsen, W. L., Quay, S. C., and Khorana, H. G., 1979, Intermolecular crosslinking of fatty acyl chains in phospholipids: Use of photoactivable carbene precursors, Proc. Natl. Acad. Sci. USA 76:2595–2599.

    Article  PubMed  CAS  Google Scholar 

  • Habeeb, A. F. S. A., 1972, Reaction of protein sulfhydryl groups with Ellman’s reagent, Meth. Enzymol. 25:457–464.

    Article  CAS  Google Scholar 

  • Haest, C. W. M., Kamp, D., and Deutike, B., 1979, Topology of membrane SH-groups in the human erythrocyte. Demonstration of a nonreactive population in intrinsic proteins, Biochim. Biophys. Acta 557:363–371.

    Article  PubMed  CAS  Google Scholar 

  • Hand, E. S., and Jenks, W. P., 1962, Mechanism of the reaction of imido esters with amines, J. Am. Chem. Soc. 84:3505–3514.

    Article  CAS  Google Scholar 

  • Henderson, R., Jubb, J. S., and Whytock, S., 1978, Specific labelling of the protein and lipid on the extracellular surface of purple membrane, J. Mol. Biol. 123:259–274.

    Article  PubMed  CAS  Google Scholar 

  • Hoare, D. G., and Koshland, D. E., 1967, A method for quantitative modification and estimation of carboxylic acid groups in proteins, J. Biol. Chem. 242:2447–2453.

    PubMed  CAS  Google Scholar 

  • Hoppe, J., and Sebald, W., 1981, An essential carboxyl group for H+ conduction in the proteolipid subunit of the ATP synthase, in: Chemiosmotic Proton Circuits in Biological Membranes (V. P. Skulachev and P. C. Hinkle, eds.), Addison-Wesley Publishing Company, London, pp. 449–458.

    Google Scholar 

  • Hoyer, P. B., Owens, J. R., and Haley, B. E., 1980, The use of photoaffinity probes to elucidate molecular mechanisms of nucleotide-regulated phenomena, Ann. N.Y. Acad. Sci. 346:280–301.

    Article  PubMed  CAS  Google Scholar 

  • Hu, V. W., and Wisnieski, B. J., 1979, Photoreactive labeling of M 13 coat protein in model membranes by use of a glycolipid probe, Proc. Natl. Acad. Sci. USA 76:5460–5464.

    Article  PubMed  CAS  Google Scholar 

  • Huang, K. S., Radhakrishnan, R., Bayley, H., and Khorana, H. G., 1982, Orientation of retinal in bacteriorhodopsin as studied by cross-linking using a photosensitive analog of retinal, J. Biol. Chem. 257:13616–13623.

    PubMed  CAS  Google Scholar 

  • Hubbard, A. L., and Cohn, Z. A., 1976, Specific labels of cell surfaces, in: Biochemical Analysis of Membranes (A. H. Maddy, ed.), Wiley, New York, pp. 427–501.

    Google Scholar 

  • Iddon, V. B., Meth-Cohn, O., Criven, E. F. V., Suschitzky, H., and Gallagher, P. T., 1979, Entwicklungen in der Arylnitren-Chemie: Synthesen und Mechanismen, Angew. Chem. 91:965–982.

    Article  CAS  Google Scholar 

  • Ji, T. H., 1977, A novel approach to the identification of surface receptors. The use of photosensitive hetero-bifunctional cross-linking reagent, J. Biol. Chem. 252:1566–1570.

    PubMed  CAS  Google Scholar 

  • Ji, T. H., 1979, The application of chemical crosslinking for studies on cell membranes and the identification of surface reporters, Biochim. Biophys. Acta 559:39–69.

    Article  PubMed  CAS  Google Scholar 

  • Ji, T. H., and Ji, I., 1982, Macromolecular photoaffinity labeling with radioactive photoactivable hetero-bifunctional reagents, Anal. Biochem. 121:286–289.

    Article  PubMed  CAS  Google Scholar 

  • Johnstone, A. P., and Crumpton, M. J., 1979, Comparison of diiodosulphophenylisothiocyanate with other reagents as surface labels for lymphocytes, FEBS Lett. 108:119–123.

    Article  PubMed  CAS  Google Scholar 

  • Jørgensen, P. L., Karlish, S. J. D., and Gitler, C., 1982, Evidence for the organization of the transmembrane segments of (Na, K)-ATPase based on labeling lipid-embedded and surface domains of the α-subunit, J. Biol. Chem. 257:7435–7442.

    PubMed  Google Scholar 

  • Kampmann, L., Lepke, S., Fasold, H., Fritzsch, G., and Passow, H., 1982, The kinetics of intramolecular cross-linking of the band 3 protein in the red blood cell membrane by 4,4′-diisothiocyano dihydrostilbene-2,2′-disulfonic acid (H2DIDS), J. Membr. Biol. 70:199–216.

    Article  PubMed  CAS  Google Scholar 

  • Katre, N. V., and Stroud, R. M., 1981, A probable linking sequence between two transmembrane components of bacteriorhodopsin, FEBS Lett. 136:170–174.

    Article  CAS  Google Scholar 

  • Katre, N. V., Wolber, P. K., Stoeckenius, W., and Stroud, R. M., 1981, Attachment site(s) of retinal in bacteriorhodopsin, Proc. Natl. Acad. Sci. USA 78:4068–4072.

    Article  PubMed  CAS  Google Scholar 

  • Kempf, Ch., Brock, C., Sigrist, H., Tanner, M. J. A., and Zahler, P., 1981, Interaction of phenylisothiocyanate with human erythrocyte band 3 protein. II. Topology of phenylisothiocyanate binding sites and influence of p-sulfophenylisothiocyanate on phenylisothiocyanate modification, Biochim. Biophys. Acta 641:88–98.

    Article  PubMed  CAS  Google Scholar 

  • Kirmse, E., (ed.), 1971, Carbene Chemistry, 2nd ed., Academic Press, New York.

    Google Scholar 

  • Klip, A., and Gitler, C., 1974, Photoactive covalent labeling of membrane components from within the lipid core, Biochem. Biophys. Res. Commun. 60:1155–1162.

    Article  PubMed  CAS  Google Scholar 

  • Knauf, P. A., 1979, Erythrocyte anion exchange and the band 3 protein: Transport kinetics and molecular structure, Curr. Top. Membr. Trans. 12:251–263.

    Google Scholar 

  • Knauf, P. A., and Rothstein, A., 1980, Use of Nap-taurine as a photoaffinity probe for the human erythrocyte anion exchange system, Ann. N.Y. Acad. Sci. 346:212–231.

    Article  PubMed  CAS  Google Scholar 

  • Lanyi, J. K., and Oesterhelt, D., 1982, Identification of the retinal-binding protein in halorhodopsin, J. Biol. Chem. 257:2674–2677.

    PubMed  CAS  Google Scholar 

  • Leblanc, P., Capone, J., and Gerber, G. E., 1982, Synthesis and biosynthetic utilization of radioactive photoreactive fatty acids, J. Biol. Chem. 257:14586–14589.

    PubMed  CAS  Google Scholar 

  • Lemke, H. D., and Oesterhelt, D., 1981a, The role of tyrosine residues in the function of bacteriorhodopsin. Specific nitration of tyrosine 26, Eur. J. Biochem. 115:595–604.

    Article  PubMed  CAS  Google Scholar 

  • Lemke, H. D., and Oesterhelt, D., 1981b, Lysine 216 is a binding site of the retinyl moiety in bacteriorhodopsin, FEBS Lett. 128:255–260.

    Article  PubMed  CAS  Google Scholar 

  • Lemke, H. D., Bergmeyer, J., Sträub, J., and Oesterhelt, D., 1982, Reversible inhibition of the proton pump bacteriorhodopsin by modification of tyrosine 64, J. Biol. Chem. 257:9384–9388.

    PubMed  CAS  Google Scholar 

  • Lodish, H. F., and Rothman, J. E., 1979, The assembly of cell membranes, Sci. Am. 240:38–53.

    Article  Google Scholar 

  • Ludwig, B., Downer, N. W., and Capaldi, R. A., 1979, Labeling of cytochrome c oxidase with [35S]diazobenzenesulfonate. Orientation of this electron transfer complex in the inner mitochondrial membrane, Biochemistry 18:1401–1407.

    Article  PubMed  CAS  Google Scholar 

  • MacLennan, D. H., and Campbell, K. P., 1979, Structure, function and biosynthesis of sarcoplasmic reticulum proteins, TIBS 4:148–151.

    CAS  Google Scholar 

  • Marfey, S. P., and Tsai, K. H., 1975, Cross-linking of phospholipids in human erythrocyte membrane, Biochem. Biophys. Res. Commun. 65:31–38.

    Article  PubMed  CAS  Google Scholar 

  • Marinetti, G. V., and Love, R., 1976, Differential reaction of cell membrane phospholipids and proteins with chemical probes, Chem. Phys. Lipids 16:239–254.

    Article  PubMed  CAS  Google Scholar 

  • Mawby, W. J., and Findlay, J. B. C., 1982, Characterization and partial sequence of di-iodosulphophenyl isothiocyanate-binding peptide from human erythrocyte anion-transport protein, Biochem. J. 205:465–475.

    PubMed  CAS  Google Scholar 

  • Means, G. E., and Feeney, R. E., 1971, Chemical Modification of Proteins, Holden-Day, San Francisco.

    Google Scholar 

  • Mitchinson, C., Wilderspin, A. F., Trinnaman, B. J., and Green, N. M., 1982, Identification of a labelled peptide after stoichiometric reaction of fluorescein isothiocyanate with the Ca2+-dependent adenosine triphosphatase of sarcoplasmic reticulum, FEBS Lett. 146:87–92.

    Article  PubMed  CAS  Google Scholar 

  • Miyakawa, T., Takemoto, L. J., and Fox, C. F., 1978, Membrane permeability of bifunctional, amino site-specific, cross-linking reagents, J. Supramol. Struct. 8:303–310.

    Article  PubMed  CAS  Google Scholar 

  • Moreland, R. B., Smith, P. K., Fujimoto, E. K., and Dockter, M. E., 1982, Synthesis and characterization of N-(4-azidophenylthio)-phthalimide: A cleavable, photoactivable crosslinking reagent that reacts with sulfhydryl groups, Anal. Biochem. 121:321–326.

    Article  PubMed  CAS  Google Scholar 

  • Mullen, E., Johnson, A. H., and Akhtar, M., 1981, The identification of lysine 216 as the retinal binding residue in bacteriorhodopsin, FEBS Lett. 130:187–193.

    Article  PubMed  CAS  Google Scholar 

  • Ngo, T. T., Yam, C. F., Lenhoff, H. M., and Ivy, J., 1981, p-Azidophenylglyoxal. A heterobifunctional photoactivable cross-linking reagent selective for arginyl residues, J. Biol. Chem. 256:11313–11318.

    PubMed  CAS  Google Scholar 

  • Nicolson, G. L., and Singer, S. J., 1974, The distribution and asymmetry of mammalian cell surface saccharides utilizing ferritin-conjugated plant agglutinins as specific saccharide stains, J. Cell. Biol. 60:236–248.

    Article  PubMed  CAS  Google Scholar 

  • Nielsen, P. E., and Buchardt, O., 1982, Aryl azides as photoaffinity labels. A photochemical study of some 4-substituted aryl azides, Photochem. Photobiol. 35:317–323.

    Article  CAS  Google Scholar 

  • Op den Kamp, J. A. F., 1979, Lipid asymmetry in membranes, Annu. Rev. Biochem. 48:47–71.

    Article  PubMed  CAS  Google Scholar 

  • Ovchinnikov, Yu. A., 1982, Rhodopsin and bacteriorhodopsin: Structure—function relationships, FEBS Lett. 148:179–191.

    Article  PubMed  CAS  Google Scholar 

  • Ovchinnikov, Yu. A., Abdulaev, N. G., Feigina, M. Yu., Kiselev, A. V., and Lobanov, N. A., 1979, The structural basis of the functioning of bacteriorhodopsin: An overview, FEBS Lett. 100:219–224.

    Article  PubMed  CAS  Google Scholar 

  • Owen, M. J., Knott, J. C. A., and Crumpton, M. J., 1980, Labeling of lymphocyte surface antigens by the lipophilic, photoactivatable reagent hexanoyldiiodo-N-(4-azido-2-nitrophenyl)tyramine, Biochemistry 19:3092–3099.

    Article  PubMed  CAS  Google Scholar 

  • Passow, H., Fasold, H., Jennings, M. L., and Lepke, S., 1982, The study of the anion transport protein (band 3 protein) in the red cell membrane by means of tritiated 4,4′-diisothiocyano-dihydrostilbene-2,2′-disulfonic acid (H2DIDS), in: Chloride Transport in Biological Membranes (A. Zadunaisky, ed.), Academic Press, New York, pp. 1–31.

    Google Scholar 

  • Peach, M. E., 1974, Thiols as nucleophiles, in: The Chemistry of the Thiol Group, Part 2 (S. Patai, ed.), John Wiley and Sons, New York, pp. 721–784.

    Google Scholar 

  • Peters, K., and Richards, F. M., 1977, Chemical cross-linking: Reagents and problems in studies of membrane structure, Annu. Rev. Biochem. 46:523–551.

    Article  PubMed  CAS  Google Scholar 

  • Phillips, A. T., 1977, Differential labeling: A general technique for selective modification of binding sites, Meth. Enzymol. 46:59–69.

    Article  PubMed  CAS  Google Scholar 

  • Pick, U., and Racker, E., 1979, Inhibition of the (Ca2+) ATPase from sarcoplasmic reticulum by dicyclohexylcarbodiimide: Evidence for location of the Ca2+ binding site in a hydrophobic region, Biochemistry 18:108–113.

    Article  PubMed  CAS  Google Scholar 

  • Previero, A., Devancourt, J., Coletti-Previero, M. A., and Laursen, R. A., 1973, Solid phase sequential analysis: Specific linking of acidic peptides by their carboxyl ends to insoluble resins, FEBS Lett. 33:135–138.

    Article  CAS  Google Scholar 

  • Prochaska, L. J., Bisson, R., and Capaldi, R. A., 1980, Structure of the cytochrome c oxidase complex: Labeling by hydrophilic and hydrophobic protein modifying reagents, Biochemistry 19:3174–3179.

    Article  PubMed  CAS  Google Scholar 

  • Prochaska, L. J., Bisson, R., Capaldi, R. A., Steffens, G. C. M., and Buse, G., 1981, Inhibition of cytochrome c oxidase function by dicyclohexylcarbodiimide, Biochim. Biophys. Acta 637:360–373.

    Article  PubMed  CAS  Google Scholar 

  • Quaroni, A., and Semenza, G., 1976, Partial amino acid sequences around the essential caroboxylate in the active sites of the intestinal sucrase isomaltase complex, J. Biol. Chem. 251:3250–3253.

    PubMed  CAS  Google Scholar 

  • Quay, S. C., Radhakrishnan, R., and Khorana, H. G., 1981, Incorporation of photosensitive fatty acids into phospholipids of Escherichia coli and irradiation-dependent cross-linking of phospholipids to membrane proteins, J. Biol. Chem. 256:4444–4449.

    PubMed  CAS  Google Scholar 

  • Radhakrishnan, R., Robson, R. J., Takagaki, Y., and Khorana, H. G., 1981, Synthesis of modified fatty acids and glycerophospholipid analogs, Meth. Enzymol. 72:408–433.

    Article  PubMed  CAS  Google Scholar 

  • Raftery, M. A., Witzemann, V., and Blanchoud, S. G., 1980, The use of photochemical probes for studies of structure and function of purified acetylcholine receptor preparations, Ann. N.Y. Acad. Sci. 346:458–474.

    Article  PubMed  CAS  Google Scholar 

  • Ramjeesingh, M., Gaarn, A., and Rothstein, A., 1980, The location of a disulfonic stilbene binding site in band 3, the anion transport protein of the red blood cell membrane, Biochim. Biophys. Acta 599:127–139.

    Article  PubMed  CAS  Google Scholar 

  • Ramjeesingh, M., Gaarn, A., and Rothstein, A., 1981, The amino acid conjugate formed by the interaction of the anion transport inhibitor 4,4′-diisothiocyano-2,2′-stilbenedisulfonic acid (DIDS) with band 3 protein from human red blood cell membranes, Biochim. Biophys. Acta 641:173–182.

    Article  PubMed  CAS  Google Scholar 

  • Renthal, R., Dawson, N., Tuley, J., and Horowitz, P., 1983, Constraints on the flexibility of bacterio-rhodopsin’s carboxyl-terminal tail at the purple membrane surface, Biochemistry 22:5–12.

    Article  PubMed  CAS  Google Scholar 

  • Riordan, J. F., 1979, Arginyl residues and anion binding sites in proteins, Mol. Cell. Biochem. 26:71–92.

    Article  PubMed  CAS  Google Scholar 

  • Ross, A. H., Radhakrishnan, R., Robson, R. J., and Khorana, H. G., 1982, The transmembrane domain of glycophorin A as studied by crosslinking using photoactivatable phospholipids, J. Biol. Chem. 257:4152–4161.

    PubMed  CAS  Google Scholar 

  • Rothstein, A., 1982, Functional structure of band 3, the anion transport protein of the red blood cell, as determined by proteolytic and chemical cleavages, in: Membranes and Transport, Vol. 2 (A. Martonosi, ed.), Plenum Press, New York, pp. 435–440.

    Google Scholar 

  • Sabban, E., Marchesi, V., Adesnik, M., and Sabatini, D. D., 1981, Erythrocyte membrane protein band 3: Its biosynthesis and incorporation into membranes, J. Cell. Biol. 91:637–646.

    Article  PubMed  CAS  Google Scholar 

  • Schäfer, R., Hinnen, R., and Franklin, R. M., 1974, Structure and synthesis of a lipid-containing bacteriophage. Properties of the structural proteins and distribution of the phospholipid, Eur. J. Biochem. 50:15–27.

    Article  PubMed  Google Scholar 

  • Schellenberg, K., 1963, The synthesis of secondary and tertiary amines by borohydride reduction, J. Org. Chem. 28:3259–3261.

    Article  CAS  Google Scholar 

  • Schweizer, E., Angst, W., and Lutz, H. U., 1982, Glycoprotein topology on intact human red blood cells reevaluated by cross-linking following amino group supplementation, Biochemistry 21:6807–6818.

    Article  PubMed  CAS  Google Scholar 

  • Seelig, J., and Seelig, A., 1980, Lipid conformation in model membranes and biological membranes, Q. Rev. Biophys. 13:19–61.

    Article  PubMed  CAS  Google Scholar 

  • Shaw, A. B., and Marinetti, G. V., 1980, Cross-linking of erythrocyte membrane proteins and phospholipids by chemical probes, Membr. Biochem. 3:1–19.

    Article  PubMed  CAS  Google Scholar 

  • Ship, S., Shami, Y., Breuer, W., and Rothstein, A., 1977, Synthesis of tritiated 4,4′-diisothiocyano-2,2′-stilbene disulfonic acid (H2DIDS) and its covalent reaction with sites related to anion transport in red blood cells, J. Membr. Biol. 33:311–324.

    Article  PubMed  CAS  Google Scholar 

  • Sigman, D. S., and Mooser, G., 1975, Chemical studies of enzyme active sites, Annu. Rev. Biochem. 44:889–931.

    Article  CAS  Google Scholar 

  • Sigrist, H., and Zahler, P., 1982a, Hydrophobic labeling and cross-linking of membrane proteins, in: Membranes and Transport, Vol. 1 (A. N. Martonosi, ed.), Plenum Press, New York, pp. 173–184.

    Chapter  Google Scholar 

  • Sigrist, H., and Zahler, P., 1982b, Heterobifunctional crosslinking of bacteriorhodopsin by hydrophobic azidoarylisothiocyanates, Meth. Enzymol. 88:207–212.

    Article  CAS  Google Scholar 

  • Sigrist, H., Kempf, Ch., and Zahler, P., 1980, Interaction of phenylisothiocyanate with human erythrocyte band 3: I. Covalent modification and inhibition of phosphate transport, Biochim. Biophys. Acta 597:137–144.

    Article  PubMed  CAS  Google Scholar 

  • Sigrist, H., Allegrini, P. R., Strasser, R. J., and Zahler, P., 1981, Chemical modification of bacteriorhodopsin by phenylisothiocyanate: Effect on the photocycle, in: The Blue Light Syndrome (H. Senger, ed.), Springer Verlag, Berlin, pp. 30–37.

    Google Scholar 

  • Sigrist, H., Allegrini, P. R., Kempf, Ch., Schnippering, Ch., and Zahler, P., 1982, 5-Isothiocyanato-1-naphthalene azide and p-azidophenylisothiocyanate: Synthesis and application in hydrophobic heterobifunctional photoactive cross-linking of membrane proteins, Eur. J. Biochem. 125:197–201.

    Article  PubMed  CAS  Google Scholar 

  • Sigrist, H., Allegrini, P. R., Stauffer, K., Schaller, J., Abdulaev, N. G., Rickli, E. E., and Zahler, P., 1984, Group-directed modification of bacteriorhodopsin by arylisothiocyanates. J. Mol. Biol. 173:93–108.

    Article  PubMed  CAS  Google Scholar 

  • Sigrist-Nelson, K., and Azzi, A., 1979, The proteolipid subunit of the chloroplast adenosine triphosphatase complex: Mobility, accessibility and interaction studied by a spin label technique, J. Biol. Chem. 254:4470–4474.

    PubMed  CAS  Google Scholar 

  • Sigrist-Nelson, K., and Azzi, A., 1980, The proteolipid subunit of the chloroplast adenosine triphosphatase complex, J. Biol. Chem. 255:10638–10643.

    PubMed  CAS  Google Scholar 

  • Spiess, M., Brunner, J., and Semenza, G., 1982, Hydrophobic labeling isolation and partial characterization of the NH2-terminal membraneous segment of sucrase—isomaltase complex, J. Biol. Chem. 257:2370–2377.

    PubMed  CAS  Google Scholar 

  • Staros, J. V., and Richards, F. M., 1974, Photochemical labeling of the surface proteins of human erythrocytes, Biochemistry 13:2720–2727.

    Article  PubMed  CAS  Google Scholar 

  • Staros, J. V., Morgan, D. G., and Appling, D. R., 1981, A membrane-impermeant, cleavable cross-linker. Dimers of human erythrocyte band 3 subunits cross-linked at the extracytoplasmic membrane face, J. Biol. Chem. 256:5890–5893.

    PubMed  CAS  Google Scholar 

  • Stauffer, K., Sigrist, H., and Zahler, P., 1982, Azo dye labeling of bacteriorhodopsin, Experientia 38:733.

    Google Scholar 

  • Steck, T. L., and Dawson, G., 1974, Topographical distribution of complex carbohydrates in the erythrocyte membrane, J. Biol. Chem. 249:2135–2142.

    PubMed  CAS  Google Scholar 

  • Steck, T. L., Ramos, B., and Strapazon, E., 1976, Proteolytic dissection of band 3, the predominant transmembrane Polypeptide of the human erythrocyte membrane, Biochemistry 15:1154–1161.

    Article  CAS  Google Scholar 

  • Stoffel, W., Salm, K. P., and Müller, M., 1982, Syntheses of phosphatidylcholines, sphingomyelines and cholesterol substituted with azido fatty acids, Hoppe-Seyler’s Z. Physiol. Chem. 363:1–18.

    Article  PubMed  CAS  Google Scholar 

  • Stuchbury, T., Shipton, M., Norris, R., Malthouse, J. P. G., Brocklehurst, K., Herbert, J. A. L., and Suschitzky, H., 1975, A reporter group delivery system with both absolute and selective specificity for thiol groups and an improved fluorescent probe containing the 7-nitrobenzo-2-oxa-1,3-diazole moiety, Biochem. J. 151:417–432.

    PubMed  CAS  Google Scholar 

  • Tarrab-Hazdai, R., Bercovici, T., Goldfarb, V., and Gitler, C., 1980, Identification of the acetylcholine receptor subunit in the lipid bilayer of Torpedo electric organ excitable membranes, J. Biol. Chem. 255:1204–1209.

    PubMed  CAS  Google Scholar 

  • Vallee, B. L., and Riordan, J. F., 1969, Chemical approaches to the properties of active sites of enzymes, Annu. Rev. Biochem. 38:733–794.

    Article  PubMed  CAS  Google Scholar 

  • Van Deenen, L. L. M., 1981, Topology and dynamics of phospholipids in membranes, FEBS Lett. 123:3–15.

    Article  PubMed  Google Scholar 

  • Van den Bosch, H., 1980, Intracellular phospholipases A, Biochim. Biophys. Acta 604:191–246.

    PubMed  Google Scholar 

  • Vanin, E. F., and Ji, T. H., 1981, Synthesis and application of cleavable photoactivable heterobifunctional reagents, Biochemistry 20:6754–6760.

    Article  PubMed  CAS  Google Scholar 

  • Verkleij, A. J., Zwaal, R. F. A., Roelofsen, B., Comfurius, P., Kastelijn, D., and Van Deenen, L. L. M., 1973, The asymmetric distribution of phospholipids in the human red cell membrane, Biochim. Biophys. Acta 323:178–193.

    Article  PubMed  CAS  Google Scholar 

  • Wang, K., and Richards, F. M., 1975, Reaction of dimethyl-3,3′-dithiobispropionimidate with intact human erythrocytes. Cross-linking of membrane proteins and hemoglobin, J. Biol. Chem. 250:6622–6626.

    PubMed  CAS  Google Scholar 

  • Wells, E., and Findlay, J. B. C., 1979, Labelling of the intramembraneous region of the major sialoglycoprotein of human erythrocytes with a photosensitive hydrophobic probe, Biochem. J. 179:265–272.

    PubMed  CAS  Google Scholar 

  • Wells, E., and Findlay, J. B. C., 1980, The isolation of human-erythrocyte band-3 Polypeptide labelled with a photosensitive hydrophobic probe, Biochem. J. 187:719–725.

    PubMed  CAS  Google Scholar 

  • Wieth, J. O., Bjerrum, P. J., and Borders, C. L., 1982, Irreversible inactivation of red cell chloride exchange with phenylglyoxal, an arginine-specific reagent, J. Gen. Physiol. 79:283–312.

    Article  PubMed  CAS  Google Scholar 

  • Wisnieski, B. J., and Bramhall, J. S., 1981, Photolabeling of cholera toxin subunits during membrane penetration, Nature 289:319–321.

    Article  PubMed  CAS  Google Scholar 

  • Wisnieski, B. J., Shiflett, M. A., Mekalanos, J., and Bramhall, J. S., 1979, Analysis of transmembrane dynamics of cholera toxin using photoreactive probes, J. Supramol. Struct. 10:191–197.

    Article  PubMed  CAS  Google Scholar 

  • Wold, F., 1972, Bifunctional reagents, Meth. Enzymol. 25:623–651.

    Article  CAS  Google Scholar 

  • Yip, C. C., Moule, M. L., and Yeung, C. W. T., 1982, Subunit structure of insulin receptor of rat adipocytes as demonstrated by photoaffinity labeling, Biochemistry 21:2940–2945.

    Article  PubMed  CAS  Google Scholar 

  • Yoshida, M., Allison, W. S., Esch, F. S., and Futai, M., 1982, The specificity of carboxyl group modification during the inactivation of the Escherichia coli F1-ATPase with dicyclohexyl[14C]carbodiimide, J. Biol. Chem. 257:10033–10037.

    PubMed  CAS  Google Scholar 

  • Zahler, P., and Wolf, M., 1982, Side-specific transfer of membrane-bound phospholipase A2 to other membranes by fusion, in: Protides of the Biological Fluids, Vol. 29 (H. Peeters, ed.), Pergamon Press, Oxford, pp. 267–270.

    Google Scholar 

  • Zaki, L., 1983, Anion transport in red blood cells and arginine specific reagents. (1) Effect of chloride and sulfate ions on phenylglyoxal sensitive sites in the red blood cell membrane, Biochem. Biophys. Res. Commun. 110:616–624.

    Article  PubMed  CAS  Google Scholar 

  • Zisapel, N., and Littauer, U. Z., 1978, A cationic hydroxysuccinimide ester. A reagent for labeling exterior membrane proteins, Biochim. Biophys. Acta 512:156–162.

    Article  PubMed  CAS  Google Scholar 

  • Zwaal, R. F. A., and Roelofsen, B., 1976, Applications of pure phospholipases in membrane studies, in: Biochemical Analysis of Membranes (A. H. Maddy, ed.), Chapman and Hall, London, pp. 352–377.

    Google Scholar 

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Sigrist, H., Zahler, P. (1985). Selective Covalent Modification of Membrane Components. In: Martonosi, A.N. (eds) The Enzymes of Biological Membranes. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4598-5_10

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