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Volumn 59, Issue 2, 1996, Pages 161-168

A new type of major aminopeptidase in bovine brain

Author keywords

[No Author keywords available]

Indexed keywords

AMINOPEPTIDASE;

EID: 0030450387     PISSN: 10773150     EISSN: None     Source Type: Journal    
DOI: 10.1006/bmme.1996.0082     Document Type: Article
Times cited : (3)

References (36)
  • 1
    • 0014498468 scopus 로고
    • Brain arylamidase. Purification and characterization of the soluble bovine enzyme
    • 1. Brecher AS, Suszkiw JB. Brain arylamidase. Purification and characterization of the soluble bovine enzyme. Biochem J 112:335-342, 1969.
    • (1969) Biochem J , vol.112 , pp. 335-342
    • Brecher, A.S.1    Suszkiw, J.B.2
  • 2
    • 0017355752 scopus 로고
    • Purification and characterization of arylamidase from monkey brain
    • 2. Hayashi M, Oshima K. Purification and characterization of arylamidase from monkey brain. J Biochem 81:631-639, 1977.
    • (1977) J Biochem , vol.81 , pp. 631-639
    • Hayashi, M.1    Oshima, K.2
  • 3
    • 0018156231 scopus 로고
    • Monkey brain arylamidase. II. Further characterization and studies on mode of hydrolysis of physiologically active peptides
    • 3. Hayashi M. Monkey brain arylamidase. II. Further characterization and studies on mode of hydrolysis of physiologically active peptides. J Biochem 84:1363-1372, 1978.
    • (1978) J Biochem , vol.84 , pp. 1363-1372
    • Hayashi, M.1
  • 4
    • 0020518554 scopus 로고
    • A major metabolite of arginine vasopressin in the brain is a highly potent neuropeptide
    • 4. Burbach JPH, Kovacs GL, Wied DD. A major metabolite of arginine vasopressin in the brain is a highly potent neuropeptide. Science 221:1310-1312, 1983.
    • (1983) Science , vol.221 , pp. 1310-1312
    • Burbach, J.P.H.1    Kovacs, G.L.2    Wied, D.D.3
  • 5
    • 0021880607 scopus 로고
    • Degradation of kyotorphin by a purified membrane-bound-amino-peptidase from monkey brain: Potentiation of kyotorphin-induced analgesia by a highly effective inhibitor, bestatin
    • 5. Ueda H, Ming G, Hazato T, Katayama T, Takagi H. Degradation of kyotorphin by a purified membrane-bound-amino-peptidase from monkey brain: Potentiation of kyotorphin-induced analgesia by a highly effective inhibitor, bestatin. Life Sci 36:1865-1871, 1985
    • (1985) Life Sci , vol.36 , pp. 1865-1871
    • Ueda, H.1    Ming, G.2    Hazato, T.3    Katayama, T.4    Takagi, H.5
  • 6
    • 0025999111 scopus 로고
    • Identification and characterization of two distinct kyotorphin-hydrolyzing enzymes in rat brain
    • 6. Akasaki K, Nakamura A, Shiomi H, Tsuji H. Identification and characterization of two distinct kyotorphin-hydrolyzing enzymes in rat brain. Neuropeptide 20:103-107, 1991.
    • (1991) Neuropeptide , vol.20 , pp. 103-107
    • Akasaki, K.1    Nakamura, A.2    Shiomi, H.3    Tsuji, H.4
  • 7
    • 0023677326 scopus 로고
    • Rationalization of aminopeptidase activities in human skeletal muscle soluble extract
    • 7. Lauffart B, Mantle D. Rationalization of aminopeptidase activities in human skeletal muscle soluble extract. Biochim Biophys Acta 956:300-306, 1988.
    • (1988) Biochim Biophys Acta , vol.956 , pp. 300-306
    • Lauffart, B.1    Mantle, D.2
  • 8
    • 0023447871 scopus 로고
    • Human skeletal muscle contains two major aminopeptidases: An anion-activated aminopeptidase B and an aminopeptidase M-like enzyme
    • 8. Ishiura S, Yamamoto T, Yamamoto M, Nojima M, Aoyagi T, Sugita H. Human skeletal muscle contains two major aminopeptidases: An anion-activated aminopeptidase B and an aminopeptidase M-like enzyme. J Biochem 102:1023-1031, 1987.
    • (1987) J Biochem , vol.102 , pp. 1023-1031
    • Ishiura, S.1    Yamamoto, T.2    Yamamoto, M.3    Nojima, M.4    Aoyagi, T.5    Sugita, H.6
  • 9
    • 0021950945 scopus 로고
    • Purification and characterization of two Cl -activated aminopeptidases hydrolysing basic termini from human skeletal muscle
    • 9. Mantle D, Lauffart B, McDermott JR, Kidd AM, Pennington RJT. Purification and characterization of two Cl -activated aminopeptidases hydrolysing basic termini from human skeletal muscle. Eur J Biochem 147:307-312, 1985.
    • (1985) Eur J Biochem , vol.147 , pp. 307-312
    • Mantle, D.1    Lauffart, B.2    McDermott, J.R.3    Kidd, A.M.4    Pennington, R.J.T.5
  • 11
    • 0022973728 scopus 로고
    • Immunoaffinity purification and characterization of leucine aminopeptidase from human liver
    • 11. Kohno H, Kanda S, Kanno T. Immunoaffinity purification and characterization of leucine aminopeptidase from human liver. J Biol Chem 261:10744-10748, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 10744-10748
    • Kohno, H.1    Kanda, S.2    Kanno, T.3
  • 12
    • 0020662674 scopus 로고
    • Participation of both 'enkephalinase' and aminopeptidase activities in the metabolism of endogenous enkephalins
    • 12. Baume SDL, Yi CC, Schwartz JC, Chaillet P, Marcais-Collado H, Costentin J. Participation of both 'enkephalinase' and aminopeptidase activities in the metabolism of endogenous enkephalins. Neuroscience 8:143-151, 1983.
    • (1983) Neuroscience , vol.8 , pp. 143-151
    • Baume, S.D.L.1    Yi, C.C.2    Schwartz, J.C.3    Chaillet, P.4    Marcais-Collado, H.5    Costentin, J.6
  • 13
    • 0021837446 scopus 로고
    • Distinct behavior of β-endorphin and corticotropin toward leucine aminopeptidase action
    • 13. Li CH, Chung D. Distinct behavior of β-endorphin and corticotropin toward leucine aminopeptidase action. Int J Peptide Prot Res 26:113-117, 1985.
    • (1985) Int J Peptide Prot Res , vol.26 , pp. 113-117
    • Li, C.H.1    Chung, D.2
  • 14
    • 0023038263 scopus 로고
    • Isolation and characterization of a new aminopeptidase from bovine lens
    • 14. Sharma KK, Ortwerth BJ. Isolation and characterization of a new aminopeptidase from bovine lens. J Biol Chem 261:4295-4301, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 4295-4301
    • Sharma, K.K.1    Ortwerth, B.J.2
  • 16
    • 0024382672 scopus 로고
    • Specificity of action of human brain alanyl aminopeptidase on Leuenkephalin and dynorphin-related peptides
    • 16. Gibson AM, McDermott JR, Lauffart B, Mantle D. Specificity of action of human brain alanyl aminopeptidase on Leuenkephalin and dynorphin-related peptides. Neuropeptide 13:259-262, 1989.
    • (1989) Neuropeptide , vol.13 , pp. 259-262
    • Gibson, A.M.1    McDermott, J.R.2    Lauffart, B.3    Mantle, D.4
  • 17
    • 0025781133 scopus 로고
    • Human brain leucyl aminopeptidase: Isolation, characterization and specificity against some neuropep tides
    • 17. Gibson AM, Biggins JA, Lauffart B, Mantle D, McDermott JR. Human brain leucyl aminopeptidase: Isolation, characterization and specificity against some neuropep tides. Neuropeptide 19:163-168, 1991.
    • (1991) Neuropeptide , vol.19 , pp. 163-168
    • Gibson, A.M.1    Biggins, J.A.2    Lauffart, B.3    Mantle, D.4    McDermott, J.R.5
  • 18
    • 0022257123 scopus 로고
    • Identification of aminopeptidase M as an enkephalin-inactivating enzyme in rat cerebral membranes
    • 18. Gros C, Giros B, Schwartz JC. Identification of aminopeptidase M as an enkephalin-inactivating enzyme in rat cerebral membranes. Biochemistry 24:2179-2185, 1985.
    • (1985) Biochemistry , vol.24 , pp. 2179-2185
    • Gros, C.1    Giros, B.2    Schwartz, J.C.3
  • 19
    • 0020051796 scopus 로고
    • Degradation of exogenous enkephalin in the Guinea-Pig ileum: Relative importance of aminopeptidase, enkephalinase and angiotensin converting enzyme activity
    • 19. Geary LE, Wiley KS, Scott WL, Cohen ML. Degradation of exogenous enkephalin in the Guinea-Pig ileum: Relative importance of aminopeptidase, enkephalinase and angiotensin converting enzyme activity. J Pharmacol Exp Ther 221:104-111, 1982.
    • (1982) J Pharmacol Exp Ther , vol.221 , pp. 104-111
    • Geary, L.E.1    Wiley, K.S.2    Scott, W.L.3    Cohen, M.L.4
  • 20
    • 0018772357 scopus 로고
    • Isolation and characterization of an enkephalin-degrading aminopeptidase from rat brain
    • 20. Schnebli HP, Phillipps MA, Barclay RK. Isolation and characterization of an enkephalin-degrading aminopeptidase from rat brain. Biochim Biophys Acta 569:89-98, 1979.
    • (1979) Biochim Biophys Acta , vol.569 , pp. 89-98
    • Schnebli, H.P.1    Phillipps, M.A.2    Barclay, R.K.3
  • 21
    • 0019189498 scopus 로고
    • Enkephalin inactivation by N-terminal tryosine cleavage: Purification and partial characterization of a highly specific enzyme from human brain
    • 21. Traficante LJ, Rotrosen J, Siekierski J, Tracer H, Gershon S. Enkephalin inactivation by N-terminal tryosine cleavage: Purification and partial characterization of a highly specific enzyme from human brain. Life Sci 26:1697-1706, 1980.
    • (1980) Life Sci , vol.26 , pp. 1697-1706
    • Traficante, L.J.1    Rotrosen, J.2    Siekierski, J.3    Tracer, H.4    Gershon, S.5
  • 22
    • 0019432699 scopus 로고
    • An aminopeptidase from bovine brain which catalyzes the hydrolysis of enkephalin
    • 22. Hersh LB, McKelvy JF. An aminopeptidase from bovine brain which catalyzes the hydrolysis of enkephalin. J Neurochem 36:171-178, 1981.
    • (1981) J Neurochem , vol.36 , pp. 171-178
    • Hersh, L.B.1    McKelvy, J.F.2
  • 23
    • 0019440573 scopus 로고
    • Purification and characterization of an enkephalin aminopeptidase from rat brain
    • 23. Wagner GW, Tavianini MA, Herrmann KM, Dixon JE. Purification and characterization of an enkephalin aminopeptidase from rat brain. Biochemistry 20:3884-3890, 1981.
    • (1981) Biochemistry , vol.20 , pp. 3884-3890
    • Wagner, G.W.1    Tavianini, M.A.2    Herrmann, K.M.3    Dixon, J.E.4
  • 24
    • 0019498536 scopus 로고
    • Solubilization and characterization of two rat brain membrane-bound aminopeptidases active on met-enkephalin
    • 24. Hersh LB. Solubilization and characterization of two rat brain membrane-bound aminopeptidases active on met-enkephalin. Biochemistry 20:2345-2350, 1981.
    • (1981) Biochemistry , vol.20 , pp. 2345-2350
    • Hersh, L.B.1
  • 25
    • 0020558176 scopus 로고
    • Purification and characterization of an enkephalin aminopeptidase from rat brain membranes
    • 25. Hui KS, Wang YJ, Lajtha A. Purification and characterization of an enkephalin aminopeptidase from rat brain membranes. Biochemistry 22:1062-1067, 1983.
    • (1983) Biochemistry , vol.22 , pp. 1062-1067
    • Hui, K.S.1    Wang, Y.J.2    Lajtha, A.3
  • 26
    • 0021849522 scopus 로고
    • Characterization of membrane-bound aminopeptidases from rat brain: Identification of the enkephalin-degrading aminopeptidase
    • 26. Hersh LB. Characterization of membrane-bound aminopeptidases from rat brain: Identification of the enkephalin-degrading aminopeptidase. J Neurochem 44:1427-1435, 1985.
    • (1985) J Neurochem , vol.44 , pp. 1427-1435
    • Hersh, L.B.1
  • 27
    • 0022364574 scopus 로고
    • Purification and characterization of a neuropeptide-degrading aminopeptidase from human brain
    • 27. McDermott JR, Mantle D, Lauffart B, Kidd AM. Purification and characterization of a neuropeptide-degrading aminopeptidase from human brain. J Neurochem 45:752-759, 1985.
    • (1985) J Neurochem , vol.45 , pp. 752-759
    • McDermott, J.R.1    Mantle, D.2    Lauffart, B.3    Kidd, A.M.4
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 28. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 78651153791 scopus 로고
    • Disc electrophoresis. II. Method and application to human serum proteins
    • 29. Davis BJ. Disc electrophoresis. II. Method and application to human serum proteins. Ann NY Acad Sci 121:404-427, 1964.
    • (1964) Ann NY Acad Sci , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 30
    • 0002687243 scopus 로고
    • Deblocking and subsequent microsequence analysis of N-terminally blocked proteins immobilized on PVFD membrane
    • Imahori K, Sakiyaman F, Eds.. New York: Plenum
    • 30. Tsunasawa S, Hirano H. Deblocking and subsequent microsequence analysis of N-terminally blocked proteins immobilized on PVFD membrane. In Methods in Protein Sequence Analysis (Imahori K, Sakiyaman F, Eds.). New York: Plenum, 1993, pp 45-53.
    • (1993) Methods in Protein Sequence Analysis , pp. 45-53
    • Tsunasawa, S.1    Hirano, H.2
  • 32
    • 0023444424 scopus 로고
    • Myristoylated α subunits of guanine nucleotide-binding regulatory proteins
    • 32. Buss JE, Mumby SM, Casey PJ, Gilman AG, Sefton BM. Myristoylated α subunits of guanine nucleotide-binding regulatory proteins. Biochemistry 84:7493-7497, 1987.
    • (1987) Biochemistry , vol.84 , pp. 7493-7497
    • Buss, J.E.1    Mumby, S.M.2    Casey, P.J.3    Gilman, A.G.4    Sefton, B.M.5
  • 33
  • 34
    • 0025012836 scopus 로고
    • G-protein α-subunit expression, myristoylation, and membrane association in COS cells
    • 34. Mumby SM, Heukeroth RO, Gordon JI, Gilman AG. G-protein α-subunit expression, myristoylation, and membrane association in COS cells. Proc Natl Acad Sci USA 87:728-732, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 728-732
    • Mumby, S.M.1    Heukeroth, R.O.2    Gordon, J.I.3    Gilman, A.G.4
  • 35
    • 0028180154 scopus 로고
    • 0α-mediated signaling in the Pit-1-dependent inhibition of the prolactine gene promotor
    • 0α-mediated signaling in the Pit-1-dependent inhibition of the prolactine gene promotor. J Biol Chem 269:12007-12013, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 12007-12013
    • Lew, A.M.1    Yao, H.2    Elsholtz, H.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.