Novel substrates for angiotensin I converting enzyme

Louis B. Hersh; John T. Gafford; James C. Powers; Takumi Tanaka; Ervin G. Erdös

doi:10.1016/0006-291X(83)91199-3

Novel substrates for angiotensin I converting enzyme

Louis B. Hersh
, John T. Gafford
, James C. Powers
, Takumi Tanaka
, Ervin G. Erdös

Producción científica: Article › revisión exhaustiva

19 Citas (Scopus)

Resumen

Homogenous human angiotensin converting enzyme (EC 3.4.15.1) cleaves dipeptides from the C-terminus of substrates containing a free carboxyl group. In this study we demonstrate that peptides containing a C-terminal nitrobenzylamine are also cleaved by the enzyme. The hydrolysis of these substrates is inhibited by the specific converting enzyme inhibitors captopril and MK421 as well as by anti-converting enzyme antibody. Sodium chloride accelerates the rate of hydrolysis forty-fold. The product of the reaction, an amino acid nitrobenzylamide, was identified by thin layer chromatography and high performance liquid chromatography. These results suggest that the carboxyl group is not an absolute requirement for substrate hydrolysis.

Idioma original	English
Páginas (desde-hasta)	654-659
Número de páginas	6
Publicación	Biochemical and Biophysical Research Communications
Volumen	110
N.º	2
DOI	https://doi.org/10.1016/0006-291X(83)91199-3
Estado	Published - ene 27 1983

Nota bibliográfica

Funding Information:
in part by grants from NIH, HL 16320, HL NIDA, DA 02243, and the Robert A. Welch We are grateful for the skilled assistance for the advice and help of Dr. Skidgel

Financiación

in part by grants from NIH, HL 16320, HL NIDA, DA 02243, and the Robert A. Welch We are grateful for the skilled assistance for the advice and help of Dr. Skidgel

Financiadores	Número del financiador
National Institutes of Health (NIH)
National Institute on Drug Abuse	DA 02243
National Heart, Lung, and Blood Institute (NHLBI)	R01HL016320

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Novel substrates for angiotensin I converting enzyme",

abstract = "Homogenous human angiotensin converting enzyme (EC 3.4.15.1) cleaves dipeptides from the C-terminus of substrates containing a free carboxyl group. In this study we demonstrate that peptides containing a C-terminal nitrobenzylamine are also cleaved by the enzyme. The hydrolysis of these substrates is inhibited by the specific converting enzyme inhibitors captopril and MK421 as well as by anti-converting enzyme antibody. Sodium chloride accelerates the rate of hydrolysis forty-fold. The product of the reaction, an amino acid nitrobenzylamide, was identified by thin layer chromatography and high performance liquid chromatography. These results suggest that the carboxyl group is not an absolute requirement for substrate hydrolysis.",

author = "Hersh, \{Louis B.\} and Gafford, \{John T.\} and Powers, \{James C.\} and Takumi Tanaka and Erd{\"o}s, \{Ervin G.\}",

note = "Funding Information: in part by grants from NIH, HL 16320, HL NIDA, DA 02243, and the Robert A. Welch We are grateful for the skilled assistance for the advice and help of Dr. Skidgel",

year = "1983",

month = jan,

day = "27",

doi = "10.1016/0006-291X(83)91199-3",

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AU - Hersh, Louis B.

AU - Gafford, John T.

AU - Powers, James C.

AU - Tanaka, Takumi

AU - Erdös, Ervin G.

N1 - Funding Information: in part by grants from NIH, HL 16320, HL NIDA, DA 02243, and the Robert A. Welch We are grateful for the skilled assistance for the advice and help of Dr. Skidgel

PY - 1983/1/27

Y1 - 1983/1/27

N2 - Homogenous human angiotensin converting enzyme (EC 3.4.15.1) cleaves dipeptides from the C-terminus of substrates containing a free carboxyl group. In this study we demonstrate that peptides containing a C-terminal nitrobenzylamine are also cleaved by the enzyme. The hydrolysis of these substrates is inhibited by the specific converting enzyme inhibitors captopril and MK421 as well as by anti-converting enzyme antibody. Sodium chloride accelerates the rate of hydrolysis forty-fold. The product of the reaction, an amino acid nitrobenzylamide, was identified by thin layer chromatography and high performance liquid chromatography. These results suggest that the carboxyl group is not an absolute requirement for substrate hydrolysis.

AB - Homogenous human angiotensin converting enzyme (EC 3.4.15.1) cleaves dipeptides from the C-terminus of substrates containing a free carboxyl group. In this study we demonstrate that peptides containing a C-terminal nitrobenzylamine are also cleaved by the enzyme. The hydrolysis of these substrates is inhibited by the specific converting enzyme inhibitors captopril and MK421 as well as by anti-converting enzyme antibody. Sodium chloride accelerates the rate of hydrolysis forty-fold. The product of the reaction, an amino acid nitrobenzylamide, was identified by thin layer chromatography and high performance liquid chromatography. These results suggest that the carboxyl group is not an absolute requirement for substrate hydrolysis.

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Novel substrates for angiotensin I converting enzyme

Resumen

Nota bibliográfica

Financiación

ASJC Scopus subject areas

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