Abstract
Covalent chromatography is a method for separation of molecules, based on formation of reversible covalent bonds between functional groups in molecules and complementary structures on a stationary solid phase. Covalent chromatography thus involves a synthetic step by which a solute is covalently immobilized to a solid support—the chemisorbent— later followed by chemical cleavage and regeneration of the sorbent. Only a few methods have been explored so far, and we will here deal only with chromatography of proteins and peptides.
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Purification and Isolation of Thiol-Containing Proteins and Peptides
Human plasma lecithin-cholesterol acyltransferase purified >20,000-fold from plasma where thiopropyl-Sepharose is one Chromatographic method used together with hydroxylapatite treatment; Holmqvist, L., 1987, Biochem. Biophys. Methods 14(6):323–333.
Bovine milk sulfhydryl oxidase prepared by covalent affinity chromatography; Janolino, V.G., and Swaisgood, H.E., 1990, J. Dairy Sci. 73:308–313.
Purification of penicillin acylase (EC 3.5.1.11) from E. coli; Boccu, E., Gianferrara, T., Gardossi, L., and Veronese, F. M., 1990, Farmaco 45(2):203–214.
Metallothionein (MT) and its aggregates without or with Hg or Cd isolated by covalent affinity chromatography on 5,5′-dithiobis-(2-nitrobenzoate)-substituted Sepharose; Kabzinski, A. K. M., and Paryjczak, T., 1989, Chromatographia 27(5–6):247–252.
Isolation of reduced δ-(l-α-aminoadipyl)-l-cysteinyl-d-valine from culture broths; Orford, C. D., Adlard, M. W., and Perry, D., 1991, J. Chem. Technol. Biotechnol. 50:523–533.
Purification of procollagen type II by covalent chromatography with activated thiol-Sepharose 4B; Angermann, K., and Barrach, H. I., 1979, Anal. Biochem. 94:253–258.
Covalent chromatography as a means of isolating thiol peptides from large proteins. Application to human ceruloplasmin; Rydén, L., and Norder, H., 1981, J. Chromatogr. 215:341–350.
Purification of chymopapain A from the dried latex of papaya; Baines, B., Brocklehurst, K., Carey, P. R., Jarvis, M., and Salin, E., 1986, Biochem. J. 233:119–129.
Purification of actinidin from kiwifruit; Brocklehurst, K., Baines, B., and Malt-house, J. P. G., 1981, Biochem. J. 197:739–746.
Resolution of ox liver thiol-disulfide oxidoreductases by a new application of covalent chromatography; Hillson, D. A., and Freedman, B. K., 1979, Biochem. Soc. Trans. 7:573–574.
Covalent chromatography used for studying the role of sulfhydryl groups in pig brain purine nucleoside phosphorylase, PNP; Hakim, G., Solaini, G., and Rossi, C. A., 1980, J. Solid-Phase Biochem. 5(4): 185–192.
Recent progress on the application of affinity and covalent chromatography to the purification of 1,25-dihydroxyvitamin D3 receptor from chick intestinal mucosa; Wecksler, W. R., Ross, F. P., Okamura, W. H., and Norman, A. W., 1979, in: Proceedings of the 4th Workshop on Vitamin D (Vitamin D: Basic research and Its Clinical Applications), Walter de Gruyer and Co., Berlin, pp. 663–666.
Purification of cytoplasmic aldehyde dehydrogenase by covalent chromatography on reduced thiopropyl-Sepharose 6B; Kitson, T. M., 1982, J. Chromatogr. 234: 181–186.
Resolution of protein disulfide-isomerase and glutathione-insulin transhydrogenase activities by covalent chromatography; Hillson, D. A., and Freedman, R. B., 1980, Biochem. J. 191:373–388.
Resolution of thiol-containing proteins by sequential elution; Hillson, D. A., 1981, J. Biochem. Biophys. Methods 4(2): 101–111.
Use of Covalent Chromatography for Sequential Analysis
Covalent chromatography for sequential analysis of membrane proteins; Ovchinnikov, Yu. A., and Abdulaev, N. G., 1986, in: Methods of Protein Sequence Analysis (K. A. Walsh, ed.), Humana, Clifton, New Jersey, pp. 189–209.
Covalent chromatography for localization of essential cysteine residues during structural studies of proteins; Ustinnikova, T. B., Popov, V. O., and Egorov, Ts. A., 1988, Bioorg. Khim. 14(7):905–909.
Sequence homology between potato and rabbit muscle phosphorylase; Nakano, K., Fukui, T., and Matsubara, H., 1980, J. Biochem. 87:919–927.
Use of Covalent Chromatography as a Tool in Immunoassay Techniques
Application in immunoassay techniques where a specific antibody is fixed to the matrix via a disulfide bond. A sample mixture containing antigens was passed through the column. After rinsing the column, the formed immunocomplex was released from the column by splitting the disulfide bridge with a reducing agent such as DTE; Nakano, K., Fukui, T., and Matsubara, H., 1980, J. Biochem. 89:223–229.
Immunocomplex-immobilization technique; Oscarsson, S., and Carlsson, J., 1991, Analyst 116:787–791.
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© 1993 Springer Science+Business Media New York
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Oscarsson, S., Porath, J. (1993). Covalent Chromatography. In: Ngo, T.T. (eds) Molecular Interactions in Bioseparations. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1872-7_26
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DOI: https://doi.org/10.1007/978-1-4899-1872-7_26
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