Abstract
Exopeptidases constitute a group of hydrolytic enzymes capable of cleaving the NH2- or COOH- terminal amino acids of peptides or polypeptides. Despite the presence in brain of peptides with important physiological properties, the role of these hydrolases in peptide and protein turnover is still obscure. It is well known that brain proteins are in dynamic equilibrium with their environment, with the processes of synthesis matching those of degradation. Protein breakdown as a consequence is an orderly process in which different batteries of endo- and exopeptidases are linked together to form a degradative pathway leading to the liberation of smaller peptides or amino acids. So far only simple schemes can be postulated for the pathways of intracellular hydrolysis of proteins and peptides.
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References
M. Bergmann, A classification of proteolytic enzymes, Advan. Enzymol. 2:49–68 (1942).
B. Shome and M. Saffran, Peptides of the hypothalamus, J. Neurochem. 13:433–448 (1966).
S. Lande, A. B. Lerner, and V. G. Upton, Pituitary peptides. Isolation of new peptides related to β-melanocyte-stimulating hormone, J. Biol. Chem. 240:4259–4263 (1965).
Enzyme Nomenclature, Elsevier, Amsterdam (1965).
G. Gomori, Chromogenic substrates for amino peptidases, Proc. Soc. Exptl. Biol. Med. 87:559–561 (1954).
J. K. McDonald, F. H. Leibach, R. E. Grindeland, and S. Ellis, Purification of Dipeptidyl Aminopeptidases II (Dipeptidyl Arylamidase II) of the Anterior Pituitary Gland. Peptide and dipeptide esterase activities, J. Biol. Chem. 243:4143–4150 (1968).
E. Blum, A. I. Yakovchuk, and A. I. Yarmoskevich, Proteolytic enzymes of the brain, Bull. Biol. Med. Exptl. U.R.S.S. 1:17–18 (1936).
E. Abderhalden and G. Ceaser, Untersuchungen über das vorkommen von polypeptidasen in centralen und peripheren nerven system, Fermentforschung 16:255–262 (1940).
M.W. Kies and S. Schwimmer. Observations on proteinase in brain,J. Biol. Chem. 145:685–691 (1942).
V. E. Price, A. Meister, J. B. Gilbert, and J. P. Greenstein, Separation of dehydropeptidases and analogous L- and D-peptidases, J. Biol. Chem. 181:535–547 (1947).
E. S. Adams and E. L. Smith, Proteolytic activity of pituitary extracts, J. Biol. Chem. 191:651–664 (1951).
H. Hanson and N. Tendis, Darstellung von Zellbestandteil-präparationen aus Hirngewebe und ihre Peptidase-Aktivität im Vergleich zu Niere und Leber, Z. Ges. Inn. Med. Ihre Grenzebiete 5:224–233 (1954).
A. Pope, Quantitative distribution of dipeptidase and acetylcholinesterase in architectonic layers of rat cerebral cortex, J. Neurophysiol. 15:115–130 (1952).
A Pope, The intralaminar distribution of dipeptidase activity in human frontal isocortex, J.Neurochem. 4:31–41 (1959).
A. Pope and C. B. Anfinsen, Histochemical distribution of peptidase activity in the central nervous system of the rat, J. Biol Chem. 173:305–311 (1948).
L. L. Uzman, M. K. Rumley, and S. Van Den Noort, The substrate specificity of mouse brain peptidase activity, J. Neurochem. 6:299–310 (1961).
L. L. Uzman, M. K. Rumley, and S. Van Den Noort, Dipeptidase activity of the brain, Nature 186:559–560 (1960).
S. Van Den Noort and L. L. Uzman, Effect of metal ions on brain peptidase activity, Proc. Soc. Exptl. Biol. Med. 108:32–34 (1961).
L. L. Uzman, S. Van Den Noort, and M. K. Rumley, Properties and classification of some brain peptidases, J. Neurochem. 9:241–252 (1962).
L. L. Uzman, M. K. Rumley, and S. Van Den Noort, The inhibition of cerebral diglycinase by α-amino, α-keto and α-hydroxy acids, J. Neurochem. 10:795–804 (1963).
K. Linderstrøm-Lang, Über Darmerepsin, Z. Physiol. Chem. 182:151–174 (1929).
K. Linderstrøm-Lang and H. Holter, Studies on enzymatic histochemistry XI. The distribution of peptidase in the gastric and duodenal mucosa of the pig, Compt. Rend. Lab. Carlsberg Sern. Chim. 20:42–56 (1935).
E. L. Smith and P. H. Spackmann, Leucineaminopeptidase V. Activation, specificity, and mechanism of action, J. Biol. Chem. 212:221–229 (1955).
E. D. Wachsmuth, Untersuchungen zur Struktur der Aminopeptidase aus Partikeln von Schweinenieren, Biochem. Z. 346:467–473 (1967).
H. Hanson,in Hoppe-Segler Thierfelder Handbuch der Physiologisch- und Pathologisch-Chemischen Analyse, Vol. 6C, p. 1, Springer, Berlin (1966).
S. R. Himmelhoch and E. A. Peterson, Preparation of leucine aminopeptidase free of endopeptidase activity, Biochemistry 7:2085–2092 (1968).
I. Schecter and A. Berger, The hydrolysis of diasteroisomers of alanine peptides by carboxypeptidase A and leucine aminopeptidase, Biochemistry 5:3371–3383 (1966).
J. B. Wolff and R. A. Resnick, Aminopeptidase of the outer lens. I. Metal ion requirements and synergistic activation II Substrate specificity, Biochim. Biophys. Acta 73:588–622 (1963).
S. Fittkau, D. Glässer, and H. Hanson, Zur Aktivität und Spezifität der Leucin-aminopeptidase in Augenlinsen. Aminosäure-und Dipeptidamilide als Substrate, Z. Physiol. Chem. 322:101–111 (1960).
A. Spector, Lens aminopeptidase I. Purification and properties, J. Biol. Chem. 238:1353–1357 (1963).
A. S. Brecher, The distribution and activity of calf brain peptidases, J. Neurochem. 10:1–6 (1963).
N. Marks, R. K. Datta, and A. Lajtha, The relationship of aminotripeptidase and arylamidase to protein breakdown in the brain, in Macromolecules and the Nervous System (Z. Lodin, ed.), Excerpta Medica, Amsterdam (1968).
E. K. Patterson, S. H. Hsiao, A. Keppel, and S. Sorot, Studies on dipeptidases and aminopeptidases. II. Zonal electrophoretic separation of rat liver peptidases, J. Biol. Chem. 240:710–715 (1965).
R. L. Joseph and W. J. Saunders, Leucine aminopeptidase in extracts of swine muscle, Biochem. J. 100:827–832 (1966).
E. K. Patterson, S. H. Hsiao, and A. Keppel, Studies on dipeptidases and aminopeptidases. I. Distinction between leucine aminopeptidase and enzymes that hydrolyze L-leucyl-β-naphthylamide, J. Biol Chem. 238:3611–3620 (1963).
G. F. Bryce and B. R. Rabin, The assay and reaction kinetics of leucine aminopeptidase from swine kidney, Biochem. J. 90:509–512 (1964).
E. L. Smith and R. L. Hill, Leucine aminopeptidase, in The Enzymes, 2nd ed., Vol. 4, pp. 37–62, Academic Press, New York (1960).
E. L. Smith, Aminopeptidases, in Methods in Enzymology (S. P. Colowick and N. O. Kaplin, eds.), Vol. 2, pp. 83–114, Academic Press, New York (1955).
N. C. Davis and E. L. Smith, Partial purification and specificity of iminodipeptidase, J. Biol Chem. 200:375–384 (1953).
D. Ellis and J. S. Fruton, On the proteolytic enzymes of animal tissues. IX. Calf thymus tripeptidase, J. Biol Chem. 191:153–159 (1951).
M. Ziff and A. A. Smith, Inhibition of aminotripeptidase, Proc. Soc. Exptl. Biol Med. 80:761–764 (1952).
R. K. Datta, N. Marks, and A. Lajtha, Purification and properties of brain tripeptidase, Federation Proc. 26:452 (1967).
N. Marks, Separation of brain peptidases and proteinases, Biochem. J. 103:40–41P (1967).
N. Marks, R. K. Datta, and A. Lajtha, Partial resolution of brain arylamidases and aminopeptidases, J. Biol. Chem. 243:2882–2889 (1968).
A. S. Brecher and R. E. Sobel, Studies on ox-brain aminopeptidases, Biochem. J. 105:641–646 (1967).
S. Simmonds and N. O. Toye, The role of metal ions in the peptidase activity in E. Coli, J. Biol. Chem. 242:2086–2093 (1967).
L. Josefsson and T. Lindberg, Intestinal dipeptidases. Spectrophotometric determination and characterization of dipeptidase activity in pig intestinal mucosa, Biochim. Biophys. Acta 105:149–161 (1965).
A. Rosenberg, The Role of Metal Ions in the Catalytic Action of Peptidases, p. 14, Almquist and Wiksell, Uppsala (1960).
G. B. Robinson and B. Shaw, The hydrolysis of dipeptides by different regions of rat small intestine, Biochem. J. 77:351–356 (1960).
H. G. Wilcox and M. Fried, Studies on rat-liver glycylglycine dipeptidase, Biochem. J. 87:192–199 (1963).
H. von Euler and H. Hasselquist, Electrophoretic enzyme determinations in the blood, serum and brain of higher animals, Arch. Kemi 25:129–133 (1966).
H. von Euler, H. Hasselquist and K. Kyyroe, Electrophoretic enzyme determinations in the blood, serum and brain of higher animals, Pts. II and III, Arch. Kemi 25:151–157 and 257–262 (1966).
H. von Euler, K. Kyyroe, and H. Hasselquist, Electrophoretic enzyme determinations in the blood, serum and brain of higher animals, Pt. IV, Arch. Kemi 25: 97–107 (1966).
A. Nishi, Inhibition of yeast glycylglycine dipeptidase by amino acids, J. Biochem. Tokyo 47:47–59 (1959).
L. T. Graham, R. P. Shank, R. Werman, and M. H. Aprison, Distribution of some synaptic transmitters in cat spinal cord: Glutamic acid, aspartic acid, γ-aminobutyric acid, glycine and glutamine, J. Neurochem. 14:465–472 (1967).
D. R. Curtis, L. Hösli, and G. A. R. Johnston, A pharmacological study of the depression of spinal neurons by glycine and related amino acids, Exptl Brain Res. 6:1–18 (1968).
A. S. Brecher and I. R. Koski, Studies on mammalian dipeptidases, Arch. Intern. Physiol. Biochem. 75:821–834 (1968).
A. Meister, Biochemistry of the Amino Acids, 2nd ed., Vol. 1, p. 119, Academic Press, New York (1965).
E. A. Hosein and M. Smart, The presence of anserine and carnosine in brain tissue, Can. J. Biochem. Physiol. 38:569–573 (1960).
T. Nakajima, F. Wolfgram, and W. G. Clark, The isolation of homoanserine from bovine brain, J. Neurochem. 14:1107–1112 (1967).
D. Araham, J. J. Pisano, and S. Udenfriend, Uptake of carnosine and homocarnosine by rat brain slices, Arch. Biochem. Biophys. 104:160–165 (1964).
D. J. McCorquodale, Some properties of a ribosomal cysteinylglycinase in Escherichia Coli B, J. Biol. Chem. 238:3914–3920 (1963).
F. Binkley, Purification and properties of renal glutathionase, J. Biol. Chem. 236:1075–1082 (1961).
A. T. Matheson and T. Murayama, The limited release of ribosomal peptidase during formation of Escherichia coli spheroplasts, Can. J. Biochem. 44:1407–1415 (1966).
P. J. Fodor, A. Miller, A. Neidle, and H. Waelsch, Enzymatic synthesis of glutathione by a transfer reaction, J. Biol. Chem. 203:991–1002 (1953).
E. L. Smith, Peptide bond cleavage (survey), in The Enzymes (P. D. Bpyer, H. Lardy, and K. Myrback, eds.), Vol. 4, pp. 1–10, Academic Press, New York (1960).
S. Sand, A. Berger, and E. Katchalski, Proline iminopeptidase. II. Purification and comparison with iminodipeptidade (prolinase), J. Biol. Chem. 237:2207–2212 (1962).
R. U. Margolis, Acid mucopolysaccharides and proteins of bovine whole brain, white matter and myelin, Biochim. Biophys. Acta 141:91–102 (1968).
E. Roboz, N. Henderson, and N. W. Klies, A collagen-like compound isolated from bovine spinal cord, J. Neurochem. 2:254–259 (1958).
J. J. Hutton, A. Marglin, B. Witkop, J. Kurz, A. Berger, and S. Udenfriend, Synthetic polypeptidases as substrates and inhibitors of collagen proline hydroxylase, Arch. Biochim. Biophys. 125:779–785 (1968).
E. R. Einstein, J. Csejtey, W. J. Davis, A. Lajtha, and N. Marks, Enzymic degradation of the encephalitogenic protein, Intern. Arch. Allergy Appl. Immunol. 34 (in press).
J. D. Padayatty and H. V. Kley, Studies on E-Peptidase, Biochemistry 5:1394–1399 (1966).
R. L. Friede, Topographic Brain Chemistry, Academic Press, New York (1966).
M.S. Burstone, Enzyme Histochemistry and Its Application in the Study of Neoplasm, Academic Press, New York (1962).
H. Tuppy, U. Wiesbauer, and E. Wintersberger, Aminosäure-p-nitroanilide als Substrate für Aminopeptidasen und andere proteolytische Fermente, Z. Physiol. Chem. 329:278–288 (1962).
S. Ellis, A thiol activated aminopeptidase of the pituitary, Biochim. Biophys. Res. Commun. 12:452–456 (1963).
A. Szewczuk, M. Kochman, and T. Baranowski, Dipeptide nitriles as substrates for colorimetric determination of aminopeptidases, Acta Biochim. Polon 12:357–367 (1965).
V. K. Hcpsu, K. K. Mäkinen, and G. G. Glenner, Purification of a mammalian peptidase selective for N-terminal arginine and lysine residues: Aminopeptidase B, Arch. Biochem. Biophys. 114:557–566 (1966).
E. E. Smith and A. M. Rutenberg, Starch gel electrophoresis of human tissue enzymes which hydrolyze L-leucyl-β-naphthylamide, Science 152:1256–1257 (1966).
G. G. Glenner, P. J. McMillan, and J. E. Folk, A mammalian peptidase specific for the hydrolysis of N-terminal α-1-glutamyl and aspartyl residues, Nature 194:867 (1962).
G. G. Glenner and J. E. Folk, Glutamyl peptidases in rat and guinea pig kidney slices, Nature 192:338–340 (1962).
I. Nagatsu, L. Gillespie, J. M. George, J. E. Folk, and G. G. Glenner, Serum amino peptidases, “angiotensinase” and hypertension. II. Amino acid β-naphthylamide hydrolysis by normal and hypertensive serum, Biochem. Pharmacol. 14:853–857 (1965).
I. Nagatsu and J. Hara, Relationship between parathyroid function and serum aminopeptidase A. activity, Nature 213:206–207 (1967).
I. Nagatsu, T. Nagatsu, and G. G. Glenner, Species difference of serum amino acid-β-naphthylamidases, Enyzmologica 34:73–76 (1968).
P. A. Khairallah and I. H. Page, Plasma angiotensinases, Biochem. Med. 1:1–8 (1967).
R. Hess, Arylamidase activity related to angiotensinase, Biochim. Biophys. Acta 99:316–324 (1965).
D. Regoli, B. Riniker, and H. Brunner, The enzymatic degradation of various angiotensin. II. derivatives by serum, plasma or kidney homogenate, Biochem. Pharmacol. 12:637–646 (1963).
D. C. Johnson and J. W. Ryan, Degradation of angiotensin-II by a carboxypeptidase of rabbit liver, Biochim. Biophys. Acta 160:196–203 (1968).
H. Y. T. Yang and E. G. Erdos, T. S. Chiang, New enzymatic route for the inactivation of angiotensin, Nature 218:1224–1226 (1968).
Z. Albert, M. Orlowski, Z. Rzucidlo, and J. Orlowska, Studies on γ-glutamyl transpeptidase activity and its histochemical location in the central nervous system of man and different animal species, Acta Histochem. 25:312–320 (1966).
J. S. Fruton, Cathepsins, in The Enzymes (P. D. Boyer, H. Lardy, and K. Myrback, eds.), pp. 233–241, Academic Press, New York (1960).
H. Wurtz, A. Tanaka, and J. S. Fruton, Polymerisation of dipeptide anides by cathepsin C, Biochemistry 1:19–28 (1962).
H. McIlwain and M. A. Trezize, The speed of several cerebral reactions involving the nicotinamide coenzymes, Biochem. J. 65:288–296 (1957).
Y. Kakimoto, T. Nakajima, A. Kanazawa, M. Takesada, and I. Sano, Isolation of γ-L-glutamyl-L-glutamic acid and γ-L-glutamyl-L-glutamine from bovine brain, Biochim. Biophys. Acta 93:333–338 (1964).
A. Kanazawa, Y. Kakimoto, T. Nakajima, H. Shimuzu, M. Takesada, and I. Sano, Isolation and identification of γ-L-glutamylglycine from bovine brain, Biochim. Biophys. Acta 97:460 (1965).
A. Z. Orlowski and A. Meister, Isolation of γ-glutamyl transpeptidase from hog kidney, J. Biol. Chem. 240:338–347 (1965).
V. K. Hopsu-Harvu, P. Rintola, and G. G. Glenner, A hog kidney aminopeptidase liberating N-terminal dipeptides. Partial purification and characterization, Acta Chem. Scand. 22:299–308 (1968).
S. Berl, Glutamine synthetase. Determination of its distribution in brain during development, Biochemistry 5:916–922 (1966).
J. H. Pincus and H. Waelsch, The specificity of transglutaminase I. Human haemoglobin as a substrate for the enzyme II. Structural requirements of the amine substrate Arch Biochem. Biophys. 126:34–52 (1968).
M. M. Nachlas, T. P. Goldstein, and A. M. Seliqman, An evaluation of aminopeptidase specificity with seven chromogenic substrates, Arch. Biochem. Biophys. 97:223–231 (1962).
V. K. Hopsu, K. K. Makinen, and G. G. Glenner, Characterization of aminopeptidase B: Substrate specificity and affector studies, Arch. Biochem. Biophys. 114: 567–575 (1966).
K. K. Mäkinen and V. K. Hopsu-Havu, A simplified method for purification of rat liver aminopeptidase B, Arch. Biochem. Biophys. 118:257–258 (1967).
N. Marks, Purification and specificity of brain aminopeptidases-II, J. Biol. Chem. (to be submitted).
S. Mahavedan and A. L. Tappel, Arylamidases of rat liver and kidney, J. Biol. Chem. 242:2369–2374 (1967).
N. Marks, B. D’Monte, C. Bellman, and A. Lajtha, Protein turnover in brain mitochondrial membranes, Brain Res. 1 (in press).
R. K. Datta, N. Marks, and A. Lajtha, Exopeptidase Activities of Brain Subcellular Membrane Fractions, p. 49, First Meeting of the International Society of Neurochemistry, Strasbourg (1967).
R. K. Datta, N. Marks, and A. Lajtha, Peptide breakdown in cerebral mitochondria, Indian J. Biochem. 4:37 (1967).
G. Pfleiderer, P. G. Celliers, M. Stanulovic, E. D. Wachsmuth, H. Determan, and G. Braunitzer, Eigenschaften und analytische Anwendung der aminopeptidase aus Nierenpartikeln, Biochem. Z. 340:552–564 (1964).
C. W. M. Adams and G. G. Glenner, Histochemistry of myelin-IV. Aminopeptidase activity in CNS and PNS, J. Neurochem. 9:233–239 (1962).
A. S. Brecher and S. W. Barefoot, The distribution of arylamidase activity in brain, Arch. Intern Physiol. Biochem. 75:816–820 (1967).
K. Felgenhauer and G. G. Glenner, The enzymatic hydrolysis of amino acid-β-naphthylamides. II. Partial purification and properties of a particle-bound cobaltactivated rat kidney aminopeptidase, J. Histochem. Cytochem. 14:401–413 (1966).
B. Sylven and U. Lippi, The suggested lysosomal localization of aminoacyl naphthylamide splitting enzymes, Exptl. Cell Res. 40:145–147 (1965).
M. Rybak, M. Petáková, and E. Simonianová, Cleavage of glycine, alanine and leucine p-nitroanilides by some animal arylaminopeptidases, Collection Czech. Chem. Commun. 32:1051–1057 (1967).
F. J. Behal, R. A. Klein, and F. B. Dawson, Separation and characterization of aminopeptidase and arylamidase components of human liver, Arch. Biochem. Biophys. 115:545–554 (1966).
S. Ellis and M. Perry, Pituitary arylamidase and peptidases, J. Biol. Chem. 241:3679–3686 (1966).
H. Neurath, Carboxypeptidase A and B in The Enzymes (P. D. Boyer, H. Lardy, and K. Myrback, eds.), Vol. 4, Pt. A, pp. 11–36, Academic Press, New York (1960).
H. J. Strecker, P. Mela, and H. Waelsch, Brain thioesterases, J. Biol. Chem. 212:223–233 (1955).
F. B. Goldstein, Biosynthesis of N-acetyl-L-aspartic acid, J. Biol. Chem. 234:2702–2706 (1959).
H. C. Buniatian, V. S. Hovhannissian, and G. V. Aprikan, The participation of N-acetyl-L-aspartic in brain metabolism, J. Neurochem. 12:695–703 (1965).
S. M. Birnbaum, L. Levinlow, R. B. Kinsley, and J. P. Greenstein, Specificity of amino acid acylases, J. Biol. Chem. 194:455–470 (1952);
S. M. Birnbaum, L. Levinlow, R. B. Kinsley, and J. P. Greenstein, Specificity of amino acid acylases and in Methods in Enzymology (S. P. Colowick and N. O. Kaplan, eds.), Vol. 2, pp. 109–119, Academic Press, New York (1955).
F. B. Goldstein (personal communication).
J. R. Brown, R. N. Greenshields, M. Yamasaki, and H. Neurath, The subunit structure of bovine procarboxypeptidase A-S6. Chemical properties and enzymatic activities of the products of molecular disaggregation, Biochemistry 2:867–876 (1963).
J. W. Prahl and H. Neurath, Pancreatic enzymes of the spiny pacific dogfish-II. Procarboxypeptidase B and carboxypeptidase B, Biochemistry 5:4137–4145 (1966).
H. Neurath, Evolution of structure and function of proteases, Science 158:1638–1644 (1967).
K. S. V. Sampath-Kumar, J. B. Clegg, and K. A. Walsh, The N-terminal sequence of bovine carboxypeptidase A and its relation to zymogen activation, Biochemistry 3:1728–1732 (1964).
B. L. Vallee, Active center of carboxypeptidase A′, Federation Proc. 23:8–17 (1964).
J. E. Coleman and B. L. Vallee, Metallocarboxypeptidase-inhibitor complexes, Biochemistry 3:1874–1879 (1964).
H. Neurath, Procarboxypeptidases: Structure, mechanism of, action and phylogenetics, Proceedings of the Seventh International Congress of Biochemistry, Tokyo Symposium 3, p. 151, Science Council, Japan (1967).
R. T. Simpson and B. L. Vallee, Iodocarboxypeptidase, Biochemistry 5:1760–1767 (1966).
H. I. Lehrer, H. V. Vunakis, and G. D. Fasman, Carboxypeptidase A. Studies with poly α-amino acids, J. Biol. Chem. 240:4585–4590 (1965).
W. A. Krivoy and D. Kroeger, The preservation of bradykinin by phenolthiathines in vitro, Brit. J. Pharmacol. 22:329–341 (1964).
E. G. Erdos and H. Y. T. Yang, Hypotensive Peptides (E. G. Erdos, N. Back, and F. Sicuteri, eds.), pp. 235, Springer-Verlag, New York (1966).
E. G. Erdos, H. Y. T. Yang, L. L. Taque, and N. Manning, Carboxypeptidase in blood and other fluids-Ill, Biochem. Pharmacol. 16:1287–1298 (1967).
E. G. Erdos, Hypotensive peptides, Advan. Pharmacol. 4:1 (1966).
Symposium, Vasoactive peptides, Federation Proc. 27:49–99 (1968).
F. LaBella, S. Vivian, and G. Ceveen, Abundance of cystathione in the pineal body. Free amino acids and related compounds of bovine pineal, anterior and posterior pituitary, and brain, Biochem. Biophys. Acta 158:286–288 (1968).
C. H. Li, Current concepts on the chemical biology of pituitary hormones, Perspectives Biol. Med. 11:498–521 (1968);
also Symposium “growth hormone” (M. Sonnberg, ed.), Ann. N.Y. Acad. Sci. 148:284–571 (1968).
M. D. Hollenberg and D. B. Hope, The isolation of the native hormone-binding proteins from bovine pituitary posterior lobes. Crystallization of neurophysin-I and II as complexes with [8-arginine]-vasopressin, Biochem. J. 106:557 (1968).
M. Ginsburg and K. Jayasena, The distribution of proteins that bind hypophysial hormones, J. Physiol. 197:65–76 (1968).
E. L. Smith, Dipeptidases, in Methods in Enzymology (S. P. Colowick and N. O. Kaplan, eds.), Vol. 2, pp. 93–109, Academic Press, New York (1955).
J. I. Harris, C. H. Li, P. G. Condliffe, and N. G. Pon, Action of carboxypeptidase on hypophysial growth hormone, J. Biol. Chem. 209:133–143 (1954).
M. Sonnenberg, M. Kikutani, C. A. Free, A. C. Nadler, and J. M. Dellacha, Chemical and biological characterization of clinically active tryptic digests of bovine growth hormone, Ann. N. Y. Acad. Sci. 148:532–538 (1968).
J. Ramachandran and C. H. Li, in Advances in Enzymology (F. F. Nord, ed.), Vol. 29, pp. 391, Wiley-Interscience, New York (1967).
P. Jouan and J. C. Rocaboy, Étude de l’activité peptidasique de la glande pinéale du Porc, Compt. Rend. Soc. Biol. 160:859–862 (1966).
T. P. J. Vanha-Perttulla and V. K. Hopsu, Esterolytic and proteolytic enzymes of the rat adenohypophysis. I. Studies with homogenate and its fractions, Histochemistry 4:312–378 (1965).
T. P. J. Vanha-Perttula and V. K. Hopsu, Esterolytic and proteolytic enzymes of the rat adenohypophysis. II. Chromatographic fractionation and characterization of enzyme activities hydrolysing leucyl-β-naphthylamide, Ann. Med. Exptl. Fenniae 43:32–39 (1965).
J. K. McDonald, S. Ellis, and T. J. Reilly, Properties of dipeptidyl arylamidase I of the pituitary. Chloride and sulfhydryl activation of seryltyrosyl-β-naphthylamide, J. Biol. Chem. 241:1494–1501 (1966).
J. K. McDonald, T. J. Reilly, B. B. Zeitman, and S. Ellis, Dipeptidyl arylamidase II of the pituitary. Properties of lysylalanyl-β-naphthylamide hydrolysis: inhibition by cations, distribution in tissues, and subcellular localization, J. Biol. Chem. 243:2028–2037 (1968).
S. Ellis and J. M. Nuenke, Dipeptidyl arylamidase III of the pituitary. Purification and characterization, J. Biol. Chem. 242:4623–4629 (1968).
G. G. Glenner, L. A. Cohen, and J. E. Folk, The enzymatic hydrolysis of amino acid-β-naphthylamides. I. Preparation of amino acid and dipeptide-β-naphthylamides, J. Histochem. Cytochem. 13:57–64 (1965).
S. Kakiuchi and H. H. Tomizawa, Properties of a glucagen degrading enzyme from beef liver, J. Biol. Chem. 239:2160–2164 (1964).
R. E. Smith and M. G. Farguhar, Lysosome function in the regulation of the secretory process in cells of the anterior pituitary gland, J. Cell Biol. 31:319–347 (1966).
H. Heller and K. Lederis, Characteristics of isolated neurosecretory vesicles from mammalian neural lobes, in Neurosecretion (H. Heller and R. B. Clark, eds.), pp. 35–50, Academic Press, New York (1962).
H. Sachs, Studies on the intracellular distribution of vasopressin, J. Neurochem, 10:289–297 (1963).
C. W. M. Adams, Histochemistry of the cells in the nervous system, in Neurohistochemistry (C. W. M. Adams, ed.), pp. 253–331, Elsevier, Amsterdam (1965).
R. Ortmann, in Handbook of Physiology (J. Field, ed.) Sec. 1, Vol. II, pp. 1034, Williams and Wilkins, Baltimore (1960).
H. F. Moyano, Effects of dehydration on rats hypothalamic acid-phosphatase, Experientia 23:529–530 (1967).
Y. Arai and T. Kusama, Leucine aminopeptidase in the supraoptic and paraventricular nuclei of the hypothalamus in normal and dehydrated rats, Proc. Japan Acad. 41:734–736 (1965).
L. Avvy, Histochemical demonstration of enzymatic activities in neurosecretory centres of some homoiothermic animals, in Neurosecretion (H. Heller and R. B. Clark, eds.), pp. 215–225, Academic Press, New York (1962).
H. Tuppy, in Polypeptides which affect smooth muscles and blood vessels (M. Schachter, ed.), pp. 49–58, Pergamon Press, Oxford (1959).
K. C. Hooper, The distribution of hypothalamic peptidases in pregnant and nonpregnant dogs, Biochem. J. 90:584–587 (1964).
W. A. Krivoy, The preservation of substance P by lysergic acid diethylamide, Brit. J. Pharmacol. 12:361–364 (1957).
K. C. Hooper, The catabolism of some physiologically active polypeptides by homogenate of dog hypothalamus, Biochem. J. 83:511–517 (1962).
K. C. Hooper, The enzymatic inactivation of some physiologically active polypeptides by different parts of the nervous system, Biochem. J. 88:398–404 (1963).
A. V. Schally, E. E. Muller, A. Arimura, T. Saito, S. Sarvano, C. Y. Bowers, and S. L. Steelman Growth hormone-releasing factor (GRF): Physiological and biochemical studies with GRF preparations of bovine and porcine origin, Ann. N. Y. Acad. Sci. 148:372–373 (1968).
S. Watanabe and S. M. McCann, Localization and mechanism of action of follicle stimulating hormone-releasing factor (FSH-RF) as determined in vitro assay, Federation Proc. 26:365 (1967).
R. Deuben and J. Meites, Stimulation of pituitary growth hormone release by a hypothalamic extract in vitro, Endocrinology 74:415 (1964).
A. V. Schally, E. E. Muller, S. Sarwano, T. Saito, and T. W. Redding, In vitro studies with hypothalamic releasing factors, Federation Proc. 26:365 (1967).
L. Thieblot, P. Bastide, S. Blaise, J. Boyer, and G. Dastugue, Enzymic activities of the pineal gland, Ann. Endocrinol. 26:313–314 (1965).
W. W. Tourtellotte, A selected review of reactions of the cerebrospinal fluid to disease, inNeurological Diagnostic Techniques (W. S. Field, ed.), pp. 1–25, Charles C. Thomas, Springfield, Illinois (1968).
W. Heyde, Zur Kenntis der Proteasen der cerebrospinal flussig keit, Z.Neurol. 138:536–543 (1932).
R. Abderhalden, Vorkommen von peptidases in c.s.f., Fermentforschung 17:173 (1943).
K. Stern, A. M. Cullen, V. T. Barber, and R. Richer, Peptidases in the cerebrospinal fluid, Can. Med. Assoc. J. 63:473–476 (1950).
J. B. Green and M. Perry, Leucine aminopeptidase activity in c.s.f., Neurology 13:924–926 (1963).
L. F. Chapman and H. G. Wolff, Studies of proteolytic enzymes in cerebrospinal fluid patients with chronic schizophrenic reactions. A preliminary report, Biological Psychiatry, pp. 130–141, Grune & Stratton, New York (1959).
P. Wiechert, Vorkommen und Aktivitat von peptidasen in liquor cerebrospinalis, Acta Biol. Med. Ger. 16:11–14 (1966).
P. J. Riekkinen and U. K. Rinne, Fractionation of peptidase and esterase activities of human cerebrospinal fluid, Brain Res. 9:136–144 (1968).
A. Nakao and E. R. Einstein, Chemical and immunological studies with a dialyzable encephalitogenic compound from bovine spinal cord, Ann. N.Y. Acad. Sci. 122:171–181 (1965).
E. R. Einstein, J. Csejtey, and N. Marks, Degradation of the encephalitogen by purified brain acid proteinase, FEBS Letters 1:191–195 (1968).
G. Porcellati and R. H. S. Thompson, The effect of nerve section on the free amino acids of nervous system, J. Neurochem. 1:340–347 (1957).
R. E. McCamen and E. Robins, Quantitative biochemical studies of Wallerian degeneration in the peripheral and central nervous system-I. Chemical constituents. II. Twelve enzymes, J. Neurochem. 5:18–41 (1959).
T. Vanha-Perttula, V. K. Hopsu, and G. G. Glenner, Enzymes in hog kidney hydrolyzing amino acid naphthylamides, J. Histochem. Cytochem. 14:314–325 (1966).
V. K. Hopsu-Havu, K. K. Makinen, and G. G. Glenner, Formation of bradykinin from kalliden-10 by aminopeptidase B, Nature 212:1271–1272 (1966).
J. W. Ryan and J. K. McKenzie, Properties of renin substrate in rabbit plasma with a note on its assay, Biochem. J. 108:687–692 (1968).
L. T. Skeggs, K. E. Lentz, J. R. Kalm, and H. Hochstrasser, Kinetics of the reaction of renin with nine synthetic peptide substrates, J. Exptl. Med. 128:13–34 (1968).
Hopsu-Harvu, P. Rintola, and G. G. Glenner, A hog-kidney aminopeptidase liberating N-terminal dipeptides, Partial purification and characterization, Acta Chem. Scand. 22:299–308 (1968).
V. S. Mathur and J. M. Walker, Oxytocinase in plasma and placenta in normal and prolonged labour, Brit. Med. J. 3:96–97 (1968).
S. P. Bessman and R. Baldwin, Imidazole aminoaciduria in cerebromacular degeneration, Science 135:789–790 (1962).
A. Meister,in Biochemistry of the Amino Acids (A. Meister, ed.), 2nd ed., Academic Press, New York (1965).
A. Lajtha, Alteration and pathology of cerebral protein metabolism, Intern. Rev. Neurobiol 7:1–40 (1964).
L. Heppel, Selective release of enzymes from bacteria, Science 156:1451–1455 (1967).
A. B. Pardee, L. S. Prestidge, M. B. Whipple, and J. Dreyfuss, A binding site for sulfate and its relation to sulfate transport into Salmonella typhimuriam, J. Biol. Chem. 241:3962–3969 (1966).
J. R. Piperno and D. L. Oxender, Animo acid-binding protein released from Escherichia coli by osmotic shock, J. Biol. Chem. 241:5732–5733 (1966).
H. R. Kaback and E. R. Stadtman, Glycine uptake in Escherichia coli-II. Glycine uptake and metabolism by an isolated membrane preparation, J. Biol. Chem. 243:1390–1400 (1968).
Y. Anraku, The reaction and restoration of galactose transport in osmotically shocked cells of Escherichia coli, J. Biol. Chem. 242:793–780 (1967).
W. Kundig, S. Ghosh, and S. Roseman, Phosphate bound to histidine in a protein as an intermediate in a novel phospho-transferase system, Proc. Natl. Acad. Sci. 52:1067–1074 (1964).
E. Kennedy, Recent progress in the biochemistry of membranes, Proceedings of the Seventh International Congress of Biochemistry of the Plenary Sessions I.U.B., Vol. 36, pp. 51–62, Science Council Japan (1967).
H. N. Christensen and M. L. Rafn, Uptake of peptides by a free-cell neoplasm, Cancer Res. 12:495–497 (1952).
F. R. Leach and E. F. Snell, The absorption of glycine and alanine and their peptides by Lactobacillus casei, J. Biol. Chem. 235:3523–3531 (1960).
D. Kessel and M. Lubin, On the distinction between peptidase activity and peptide transport, Biochim. Biophys. Acta 71:656–663 (1963).
T. D. Brock and S. O. Wooley, Glycylglycine uptake in streptococci and a possible role of peptides in amino acid transport, Arch. Biochem. Biophys. 105:51–57 (1964).
J. W. Payne and C. Gilvary, Oligopeptide transport in Escherichia coli, J. Biol. Chem. 243:3395–3403 (1968).
R. K. Crane, Structure and functional organization of an epithelial cell brush border, inIntracellular Transport (K. B. Warren, ed.), pp. 71–102, Academic Press, New York (1966).
A. Eicholz, Studies on the organization of the brush border in intestinal epithelial cells-V. Subfractionation of enzymatic activities of the microvillus membrane, Biochim. Biophys. Acta 163:101–107 (1968).
P. Emmelot, and A. Visser, and E. L. Benedetti, Studies on plasma membranes-VII. A leucyl-β-naphthylamidase containing repeating units of the surface of isolated liver and hepatoma plasma membranes, Biochim. Biophys. Acta 150:364–375 (1968).
J. J. Pisano, J. D. Wilson, L. Cohen, D. Abraham, and S. Udenfriend, Isolation of γ-aminobutyrylhistidine (Homocarnosine) from brain, J. Biol. Chem. 236:499–502 (1961).
D. Abraham, J. J. Pisano, and S. Udenfriend, The distribution of homocarnosine in mammals, Arch. Biochem. Biophys. 99:210–213 (1962).
N. Marks and A. Lajtha, Protein breakdown, in Handbook of Neurochemistry (A. Lajtha, ed.), Vol. V, Plenum Press, New York (in preparation).
N. Cuzin, N. Kretchmer, R. E. Greenberg, R. Hurwitz, and F. Chapeville, Enzymatic hydrolysis of N-substitutal aminoacyl-tRNA, Proc. Natl. Acad. Sci. 58:2079–2083 (1967).
H. Kossel and U. L. RajBhandarz, Studies on polynucleotides. Enzymatic hydrolysis of N-acylaminoacyl-transfer-RNA, J. Mol. Biol. 35:539 (1968).
J. C. Brown and P. Doty, Protein factor requirement for binding of messenger RNA to ribosomes, Biochem. Biophys. Res. Commun. 30:284–291 (1968).
J. Lucas-Lenand and A. L. Haenni, Requirement of guanosine 5′-tri-phosphate for ribosomal binding of aminoacyl-L-sRNA, Proc. Natl. Acad. Sci. 59:554–559 (1968).
R. K. Datta, N. Marks, and A. Lajtha, Protein breakdown in peripheral nerve and lobster ventral cord (unpublished results), see Axoplasmic transport, Neurosci. Res. Progr. Bull. 5:(4), 341 (1968).
F. H. Leibach and F. Brinkley, γ-Glutamyl transferase of swine kidney, Arch. Biochem. Biophys. 127:292–301 (1968).
A. Yaron and D. Mylnar, Aminopeptidase P., Biochem. Biophys. Res. Commun. 32:658–663 (1968).
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Marks, N. (1970). Peptide Hydrolases. In: Lajtha, A. (eds) Metabolic Reactions in the Nervous System. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-7160-5_5
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