메뉴 건너뛰기




Volumn 279, Issue 3, 1996, Pages 1582-1589

Single-domain angiotensin I converting enzyme (kininase II): Characterization and properties

Author keywords

[No Author keywords available]

Indexed keywords

BRADYKININ; CAPTOPRIL; DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; ENALAPRILAT; KALLIKREIN; LISINOPRIL; PLASMIN; QUINAPRILAT; RAMIPRILAT; TRITIUM;

EID: 0030434802     PISSN: 00223565     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (58)

References (52)
  • 1
    • 0030027331 scopus 로고    scopus 로고
    • Acute angiotensin-converting enzyme inhibition increases the plasma level of the natural stem-cell regulator N-Acetyl-Seryl-Aspartyl-Lysyl-Proline
    • AZIZI, M., ROUSSEAU, A., EZAN, E., GUYENE, T.-T., MICHELET, S., GROCNET, J.-M., LENFANT, M., CORVOL, P. AND MÉNARD, J.: Acute angiotensin-converting enzyme inhibition increases the plasma level of the natural stem-cell regulator N-Acetyl-Seryl-Aspartyl-Lysyl-Proline. J. Clin. Invest. 97: 839-844, 1996.
    • (1996) J. Clin. Invest. , vol.97 , pp. 839-844
    • Azizi, M.1    Rousseau, A.2    Ezan, E.3    Guyene, T.-T.4    Michelet, S.5    Grocnet, J.-M.6    Lenfant, M.7    Corvol, P.8    Ménard, J.9
  • 2
    • 0024379270 scopus 로고
    • Mouse angiotensin-converting enzyme is a protein composed of two homologous domains
    • BERNSTEIN, K. E., MARTIN, B. M., EDWARDS, A. S. AND BERNSTEIN, E. A.: Mouse angiotensin-converting enzyme is a protein composed of two homologous domains. J. Biol. Chem. 264: 11945-11951, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11945-11951
    • Bernstein, K.E.1    Martin, B.M.2    Edwards, A.S.3    Bernstein, E.A.4
  • 3
    • 0025873352 scopus 로고
    • Amelioration of chemotherapy-induced toxicity by co-treatment with AcSDKP, a tetrapeptide inhibitor of hematopoietic stem cell proliferation
    • BOGDEN, A. E., CARDE, P., DESCHAMPS DE PAILLETTE, E., MOREAU, J.-P., TUBIANA, M. AND FRINDEL, E.: Amelioration of chemotherapy-induced toxicity by co-treatment with AcSDKP, a tetrapeptide inhibitor of hematopoietic stem cell proliferation. Ann. NY Acad. Sci. 628: 126-139, 1991.
    • (1991) Ann. NY Acad. Sci. , vol.628 , pp. 126-139
    • Bogden, A.E.1    Carde, P.2    Deschamps De Paillette, E.3    Moreau, J.-P.4    Tubiana, M.5    Frindel, E.6
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding
    • BRADFORD, M. M.: A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72: 248-254, 1976.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0025204149 scopus 로고
    • Essential residues in angiotensin converting enzyme: Modification with 1-fluoro-2,4-dinitrobenzene
    • BÜNNING, P., KLEEMANN, S. G. AND RIORDAN, J. F.: Essential residues in angiotensin converting enzyme: Modification with 1-fluoro-2,4-dinitrobenzene. Biochemistry 29: 10488-10492, 1990.
    • (1990) Biochemistry , vol.29 , pp. 10488-10492
    • Bünning, P.1    Kleemann, S.G.2    Riordan, J.F.3
  • 6
    • 0025222019 scopus 로고
    • Identification of essential tyrosine and lysine residues in angiotensin converting enzyme: Evidence for a single active site
    • CHEN, Y.-N. P. AND RIORDAN, J. F.: Identification of essential tyrosine and lysine residues in angiotensin converting enzyme: Evidence for a single active site. Biochemistry 29: 10493-10498, 1990.
    • (1990) Biochemistry , vol.29 , pp. 10493-10498
    • Chen, Y.-N.P.1    Riordan, J.F.2
  • 8
    • 0042908657 scopus 로고
    • Molecular cloning of human testicular angiotensin-converting enzyme: The testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme
    • EHLERS, M. R. W., Fox, E. A., STRYDOM, D. J. AND RIORDAN, J. F.: Molecular cloning of human testicular angiotensin-converting enzyme: The testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc. Natl. Acad. Sci. U.S.A. 86: 7741-7745, 1989.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 7741-7745
    • Ehlers, M.R.W.1    Fox, E.A.2    Strydom, D.J.3    Riordan, J.F.4
  • 9
    • 0002732011 scopus 로고
    • Angiotensin-converting enzyme. Biochemistry and molecular biology
    • ed. by J. H. Laragh and B. M. Brenner, 2nd ed., Raven Press, Ltd., New York
    • EHLERS, M. R. W. AND RIORDAN, J. F.: Angiotensin-converting enzyme. Biochemistry and molecular biology. In Hypertension: Pathophysiology, Diagnosis, and Management, ed. by J. H. Laragh and B. M. Brenner, 2nd ed., pp. 1217-1231, Raven Press, Ltd., New York, 1990.
    • (1990) Hypertension: Pathophysiology, Diagnosis, and Management , pp. 1217-1231
    • Ehlers, M.R.W.1    Riordan, J.F.2
  • 10
    • 0025788169 scopus 로고
    • Angiotensin converting enzyme: Zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes
    • EHLERS, M. R. W. AND RIORDAN, J. F.: Angiotensin converting enzyme: Zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes. Biochemistry 30: 7118-7126, 1991.
    • (1991) Biochemistry , vol.30 , pp. 7118-7126
    • Ehlers, M.R.W.1    Riordan, J.F.2
  • 11
    • 0025039169 scopus 로고
    • Angiotensin I converting enzyme and the changes in our concepts through the years. Lewis K. Dahl Memorial Lecture
    • ERDÖS, E.G.: Angiotensin I converting enzyme and the changes in our concepts through the years. Lewis K. Dahl Memorial Lecture. Hypertension 16: 363-370, 1990.
    • (1990) Hypertension , vol.16 , pp. 363-370
    • Erdös, E.G.1
  • 12
    • 0030075328 scopus 로고    scopus 로고
    • News about ACE, or, the separate lives of "Siamese Twin" domains
    • ERDÖS, E. G.: News about ACE, or, the separate lives of "Siamese Twin" domains (Editorial). J. Clin. Invest. 97: 588, 1996.
    • (1996) J. Clin. Invest. , vol.97 , pp. 588
    • Erdös, E.G.1
  • 13
    • 4243977947 scopus 로고
    • Inactivation and potentiation of the effects of bradykinin
    • ed. by E. G. Erdös, N. Back and F. Sicuteri, Springer-Verlag, New York
    • ERDÖS, E. G. AND YANG, H. Y. T.: Inactivation and potentiation of the effects of bradykinin. In Hypotensive Peptides, ed. by E. G. Erdös, N. Back and F. Sicuteri, Springer-Verlag, New York, pp. 235-250, 1966.
    • (1966) Hypotensive Peptides , pp. 235-250
    • Erdös, E.G.1    Yang, H.Y.T.2
  • 16
    • 0028453483 scopus 로고
    • Angiotensin converting enzyme inhibition and the heart
    • GAVRAS, H.: Angiotensin converting enzyme inhibition and the heart. Hypertension 23: 813-818, 1994.
    • (1994) Hypertension , vol.23 , pp. 813-818
    • Gavras, H.1
  • 17
    • 0027220366 scopus 로고
    • ACE inhibitors: A decade of clinical experience
    • GAVRAS, I. AND GAVRAS, H.: ACE inhibitors: A decade of clinical experience. Hosp. Pract. 28:61-71, 1993.
    • (1993) Hosp. Pract. , vol.28 , pp. 61-71
    • Gavras, I.1    Gavras, H.2
  • 18
    • 0026431315 scopus 로고
    • 3H] Ramiprilat binding to the angiotensin converting enzyme in rat renal brushborder membranes: The effect of chloride
    • 3H] Ramiprilat binding to the angiotensin converting enzyme in rat renal brushborder membranes: The effect of chloride. Eur. J. Pharmacol. 206: 203-209, 1991.
    • (1991) Eur. J. Pharmacol. , vol.206 , pp. 203-209
    • Grima, M.1    Mosser, J.2    Welsch, C.3    Barthelmebs, M.4    Imbs, J.-L.5
  • 20
    • 0019843086 scopus 로고
    • Tripeptidyl carboxypeptidase activity of kininase II (angiotensin-converting enzyme)
    • INOKUCHI, J.-I. AND NAGAMATSU, A.: Tripeptidyl carboxypeptidase activity of kininase II (angiotensin-converting enzyme). Biochim. Biophys. Acta 662: 300-307, 1981.
    • (1981) Biochim. Biophys. Acta , vol.662 , pp. 300-307
    • Inokuchi, J.-I.1    Nagamatsu, A.2
  • 21
    • 0021034757 scopus 로고
    • Rabbit pulmonary angiotensin-converting enzyme: The NH2-terminal fragment with enzymatic activity and its formation from the native enzyme by NH40H treatment
    • IWATA, K., BLACKER, R., SOPPER, R. L. AND LAI, C.-Y.: Rabbit pulmonary angiotensin-converting enzyme: The NH2-terminal fragment with enzymatic activity and its formation from the native enzyme by NH40H treatment. Arch. Biochem. Biophys. 227: 188-201, 1983.
    • (1983) Arch. Biochem. Biophys. , vol.227 , pp. 188-201
    • Iwata, K.1    Blacker, R.2    Sopper, R.L.3    Lai, C.-Y.4
  • 22
    • 0025340195 scopus 로고
    • A peptidase in human platelets that deamidates tachykinins: Probable identity with the lysosomal "protective protein"
    • JACKMAN, H. L., TAN, F., TAMEI, H., BEURLING-HARBURY, C., LI X-Y., SKIDGEL, R. A. AND ERDÖS, E. G.: A peptidase in human platelets that deamidates tachykinins: Probable identity with the lysosomal "protective protein." J. Biol. Chem. 265: 11265-11272, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11265-11272
    • Jackman, H.L.1    Tan, F.2    Tamei, H.3    Beurling-Harbury, C.4    Li, X.-Y.5    Skidgel, R.A.6    Erdös, E.G.7
  • 23
    • 0027175193 scopus 로고
    • Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other natural peptides
    • JASPARD, E., WEI, L. AND ALHENC-GELAS, F.: Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other natural peptides. J. Biol. Chem. 268: 9496-9503, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9496-9503
    • Jaspard, E.1    Wei, L.2    Alhenc-Gelas, F.3
  • 24
    • 0028998747 scopus 로고
    • Catalytic properties of the two active sites of angiotensin I-converting enzyme on the cell surface
    • JASPARD, E. AND ALHENC-GELAS, F.: Catalytic properties of the two active sites of angiotensin I-converting enzyme on the cell surface. Biochem. Biophys. Res. Commun. 211: 528-534, 1995.
    • (1995) Biochem. Biophys. Res. Commun. , vol.211 , pp. 528-534
    • Jaspard, E.1    Alhenc-Gelas, F.2
  • 25
    • 0021134710 scopus 로고
    • Enzymes in placental microvilli: Angiotensin I converting enzyme, angiotensinase A, carboxypeptidase, and neutral endopeptidase ("enkephalinase")
    • JOHNSON, A. R., SKIDGEL, R. A., GAFFORD, J. T. AND ERDÖS, E. G.: Enzymes in placental microvilli: Angiotensin I converting enzyme, angiotensinase A, carboxypeptidase, and neutral endopeptidase ("enkephalinase"). Peptides 5: 789-796, 1984.
    • (1984) Peptides , vol.5 , pp. 789-796
    • Johnson, A.R.1    Skidgel, R.A.2    Gafford, J.T.3    Erdös, E.G.4
  • 26
    • 0028332078 scopus 로고
    • Role of glycosylation in the biosynthesis and activity of rabbit testicular angiotensin converting enzyme
    • KASTURI, S., JABBAR, M. A., SEN, G. C. AND SEN, I.: Role of glycosylation in the biosynthesis and activity of rabbit testicular angiotensin converting enzyme. Biochemistry 33: 6228-6234, 1994.
    • (1994) Biochemistry , vol.33 , pp. 6228-6234
    • Kasturi, S.1    Jabbar, M.A.2    Sen, G.C.3    Sen, I.4
  • 27
    • 0024425354 scopus 로고
    • Structure of testicular angiotensin-converting enzyme. A segmental mosaic enzyme
    • KUMAR, R. S., KUSARI, J., ROY, S. N., SOFFER, R. L. AND SEN G. C.: Structure of testicular angiotensin-converting enzyme. A segmental mosaic enzyme. J. Biol. Chem. 264: 16754-16758, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16754-16758
    • Kumar, R.S.1    Kusari, J.2    Roy, S.N.3    Soffer, R.L.4    Sen, G.C.5
  • 28
    • 0025756812 scopus 로고
    • The mRNAs encoding the two angiotensin converting isozymes are transcribed from the same gene by a tissue-specific choice of alternative transcription initiation sites
    • KUMAR, R. S., THEKKUMKARA, T. J. AND SEN G. C.: The mRNAs encoding the two angiotensin converting isozymes are transcribed from the same gene by a tissue-specific choice of alternative transcription initiation sites. J. Biol. Chem. 266: 3854-3862, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3854-3862
    • Kumar, R.S.1    Thekkumkara, T.J.2    Sen, G.C.3
  • 29
    • 0024473131 scopus 로고
    • The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, non-duplicated form of the enzyme
    • LATTION, A.-L., SOUBRIER, F., ALLEGRINI, J., HUBERT, C., CORVOL, P. AND ALHENCGELAS, F.: The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, non-duplicated form of the enzyme. FEBS Lett. 252: 99-104, 1989.
    • (1989) FEBS Lett. , vol.252 , pp. 99-104
    • Lattion, A.-L.1    Soubrier, F.2    Allegrini, J.3    Hubert, C.4    Corvol, P.5    Alhencgelas, F.6
  • 30
    • 0018129118 scopus 로고
    • Subunits of human plasma kininase II generated by plasma kallikrein
    • NAKAHARA, M.: Subunits of human plasma kininase II generated by plasma kallikrein. Biochem. Pharmacol. 27:1651-1657 1978.
    • (1978) Biochem. Pharmacol. , vol.27 , pp. 1651-1657
    • Nakahara, M.1
  • 31
    • 0018089958 scopus 로고
    • Purification and properties of angiotensin I-converting enzyme from human lung
    • NISHIMURA, K., YOSHIDA, N., HIWADA, K., UEDA, E. AND KOKUBU, T.: Purification and properties of angiotensin I-converting enzyme from human lung. Jpn. Circ. J. 42: 639-640, 1978.
    • (1978) Jpn. Circ. J. , vol.42 , pp. 639-640
    • Nishimura, K.1    Yoshida, N.2    Hiwada, K.3    Ueda, E.4    Kokubu, T.5
  • 32
    • 0028174975 scopus 로고
    • From peptides to peptidases: A chronicle of drug discovery
    • ONDETTI, M. A.: From peptides to peptidases: A chronicle of drug discovery. Annu. Rev. Pharmacol. 34: 1-16, 1994.
    • (1994) Annu. Rev. Pharmacol. , vol.34 , pp. 1-16
    • Ondetti, M.A.1
  • 33
    • 0021894806 scopus 로고
    • Cleavage of des-Arg9-bradykinin by angiotensin I-converting enzyme from pig kidney cortex
    • OSHIMA, G., HIRAGA, Y., SHIRONO, K., OH-ISHI, S., SAKAKIBARA, S. AND KINOSHITA, T.: Cleavage of des-Arg9-bradykinin by angiotensin I-converting enzyme from pig kidney cortex. Experientia 41: 325-328, 1985.
    • (1985) Experientia , vol.41 , pp. 325-328
    • Oshima, G.1    Hiraga, Y.2    Shirono, K.3    Oh-Ishi, S.4    Sakakibara, S.5    Kinoshita, T.6
  • 34
    • 0021780973 scopus 로고
    • The design and properties of N-carboxyalkyldipeptide inhibitors of angiotensin converting enzyme
    • PATCHETT, A. A. AND CORDES, E. H.: The design and properties of N-carboxyalkyldipeptide inhibitors of angiotensin converting enzyme. Adv. Enzymol. Relat. Areas Mol. Biol. 57: 1-84, 1985.
    • (1985) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.57 , pp. 1-84
    • Patchett, A.A.1    Cordes, E.H.2
  • 35
    • 0028180926 scopus 로고
    • Structural constraints of inhibitors for binding at two active sites on somatic angiotensin converting enzyme
    • PERICH, R. B., JACKSON, B. AND JOHNSTON, C. I.: Structural constraints of inhibitors for binding at two active sites on somatic angiotensin converting enzyme. Eur. J. Pharmacol. 266: 201-211, 1994.
    • (1994) Eur. J. Pharmacol. , vol.266 , pp. 201-211
    • Perich, R.B.1    Jackson, B.2    Johnston, C.I.3
  • 36
    • 0028157441 scopus 로고
    • Regulated cleavage-secretion of the membrane-bound angiotensin converting enzyme
    • RAMCHANDRAN, R., SEN, G. C., MISONO, K. AND SEN, I.: Regulated cleavage-secretion of the membrane-bound angiotensin converting enzyme. J. Biol. Chem. 269: 2125-2130, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2125-2130
    • Ramchandran, R.1    Sen, G.C.2    Misono, K.3    Sen, I.4
  • 37
    • 0028967315 scopus 로고
    • The hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme
    • ROUSSEAU, A., MICHAUD, A., CHAUVET, M.-T., LENFANT, M. AND CORVOL, P.: The hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme. J. Biol. Chem. 270: 3656-3661, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3656-3661
    • Rousseau, A.1    Michaud, A.2    Chauvet, M.-T.3    Lenfant, M.4    Corvol, P.5
  • 38
    • 0023690624 scopus 로고
    • Basic carboxypeptidases: Regulators of peptide hormone activity
    • SKIDGEL, R. A.: Basic carboxypeptidases: Regulators of peptide hormone activity. Trends Pharmacol. Sci. 9: 299-304, 1988.
    • (1988) Trends Pharmacol. Sci. , vol.9 , pp. 299-304
    • Skidgel, R.A.1
  • 39
    • 0011118368 scopus 로고
    • Novel activity of human angiotensin I converting enzyme: Release of the NH2- and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone
    • SKIDGEL, R. A. AND ERDÖS, E. G.: Novel activity of human angiotensin I converting enzyme: Release of the NH2- and COOH-terminal tripeptides from the luteinizing hormone-releasing hormone. Proc. Natl. Acad. Sci. U.S.A. 82: 1025-1029, 1985.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 1025-1029
    • Skidgel, R.A.1    Erdös, E.G.2
  • 40
    • 0000401180 scopus 로고
    • Biochemistry of angiotensin converting enzyme
    • ed. by J. I. S. Robertson and M. G. Nicholls, Gower Medical Publishing, London
    • SKIDGEL, R. A. AND ERDÖS, E. G.: Biochemistry of angiotensin converting enzyme. In The Renin Angiotensin System, ed. by J. I. S. Robertson and M. G. Nicholls, vol. 1, pp. 10.1-10.10, Gower Medical Publishing, London, 1993.
    • (1993) The Renin Angiotensin System , vol.1
    • Skidgel, R.A.1    Erdös, E.G.2
  • 42
    • 0027312101 scopus 로고
    • Molecular biology of the angiotensin I converting enzyme: I. Biochemistry and structure of the gene
    • SOUBRIER, F., HUBERT, C., TESTUT, P., NADAUD, S., ALHENC-GELAS, F. AND CORVOL, P.: Molecular biology of the angiotensin I converting enzyme: I. Biochemistry and structure of the gene. J. Hypertension 11: 471-476, 1993a.
    • (1993) J. Hypertension , vol.11 , pp. 471-476
    • Soubrier, F.1    Hubert, C.2    Testut, P.3    Nadaud, S.4    Alhenc-Gelas, F.5    Corvol, P.6
  • 43
    • 0027283916 scopus 로고
    • Molecular biology of the angiotensin I converting enzyme: II. Structure-function. Gene polymorphism and clinical implications
    • SOUBRIER, F., WEI, L., HUBERT, C., CLAUSER, E., ALHENC-GELAS, F. AND CORVOL, P.: Molecular biology of the angiotensin I converting enzyme: II. Structure-function. Gene polymorphism and clinical implications. J. Hypertension 11: 599-604, 1993b.
    • (1993) J. Hypertension , vol.11 , pp. 599-604
    • Soubrier, F.1    Wei, L.2    Hubert, C.3    Clauser, E.4    Alhenc-Gelas, F.5    Corvol, P.6
  • 44
    • 0019797050 scopus 로고
    • Purification and characterization of human converting enzyme (kininase II)
    • STEWART, T. A., WEARE, J. A. AND ERDÖS, E. G.: Purification and characterization of human converting enzyme (kininase II). Peptidea 2: 145-152, 1981.
    • (1981) Peptidea , vol.2 , pp. 145-152
    • Stewart, T.A.1    Weare, J.A.2    Erdös, E.G.3
  • 45
    • 0019744505 scopus 로고
    • Human peptidyl dipeptidase (converting enzyme, kininase II)
    • STEWART, T. A., WEARE, J. A. AND ERDÖS, E. G.: Human peptidyl dipeptidase (converting enzyme, kininase II). Methods Enzymol. 80: 450-460, 1982.
    • (1982) Methods Enzymol. , vol.80 , pp. 450-460
    • Stewart, T.A.1    Weare, J.A.2    Erdös, E.G.3
  • 46
    • 0018827552 scopus 로고
    • Angiotensin I converting enzyme (kininase II) of the brush border of human and swine intestine
    • WARD, P. E., SHERIDAN, M. A., HAMMON, K. J. AND ERDÖS, E. G.: Angiotensin I converting enzyme (kininase II) of the brush border of human and swine intestine. Biochem. Pharmacol. 29: 1525-1529, 1980.
    • (1980) Biochem. Pharmacol. , vol.29 , pp. 1525-1529
    • Ward, P.E.1    Sheridan, M.A.2    Hammon, K.J.3    Erdös, E.G.4
  • 47
    • 0025739667 scopus 로고
    • The two homologous domains of human angiotensin I-converting enzyme are both catalytically active
    • WEI, L., ALHENC-GELAS, F., CORVOL, P. AND CLAUSER, E.: The two homologous domains of human angiotensin I-converting enzyme are both catalytically active. J. Biol. Chem. 266: 9002-9008, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9002-9008
    • Wei, L.1    Alhenc-Gelas, F.2    Corvol, P.3    Clauser, E.4
  • 48
    • 0026643458 scopus 로고
    • The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors
    • WEI, L., CLAUSER, E., ALHENC-GELAS, F. AND CORVOL, P.: The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors. J. Biol. Chem. 267: 13398-13405, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13398-13405
    • Wei, L.1    Clauser, E.2    Alhenc-Gelas, F.3    Corvol, P.4
  • 49
    • 0022222411 scopus 로고
    • Recent developments in the design of angiotensin-converting enzyme inhibitors
    • WYVRATT, M. J. AND PATCHETT, A. A.: Recent developments in the design of angiotensin-converting enzyme inhibitors. Med. Res. Rev. 5: 483-531, 1985.
    • (1985) Med. Res. Rev. , vol.5 , pp. 483-531
    • Wyvratt, M.J.1    Patchett, A.A.2
  • 50
    • 0014214810 scopus 로고
    • Second kininase in human blood plasma
    • YANG, H. Y. T. AND ERDÖS, E. G.: Second kininase in human blood plasma. Nature 215: 1402-1403, 1967.
    • (1967) Nature , vol.215 , pp. 1402-1403
    • Yang, H.Y.T.1    Erdös, E.G.2
  • 51
    • 0014957830 scopus 로고
    • A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin
    • YANG, H. Y. T., ERDÖS, E. G. AND LEVIN, Y.: A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin. Biochim. Biophys. Acta 214: 374-376, 1970.
    • (1970) Biochim. Biophys. Acta , vol.214 , pp. 374-376
    • Yang, H.Y.T.1    Erdös, E.G.2    Levin, Y.3
  • 52
    • 0015051857 scopus 로고
    • Characterization of a dipeptide hydrolase (kininase II; angiotenain I converting enzyme)
    • YANG, H. Y. T., ERDÖS, E. G. AND LEVIN, Y.: Characterization of a dipeptide hydrolase (kininase II; angiotenain I converting enzyme). J. Pharmacol. Exp. Ther. 177: 291-300, 1971.
    • (1971) J. Pharmacol. Exp. Ther. , vol.177 , pp. 291-300
    • Yang, H.Y.T.1    Erdös, E.G.2    Levin, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.