A new feature of angiotensin-converting enzyme in the brain: Hydrolysis of substance P

Highly purified rat brain angiotensin-converting enzyme hydrolyzes substance P which contains a C-terminal amino acid with an amidated carboxyl group. The hydrolysis of substance P verified by amino-group fluorometry and by high-performance liquid chromatography is inhibited by captopril, but not by...

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Bibliographic Details
Published inBiochemical and biophysical research communications Vol. 116; no. 2; pp. 735 - 742
Main Authors Yokosawa, Hideyoshi, Endo, Shogo, Ogura, Yasuhiko, Ishii, Shin-ichi
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 31.10.1983
Subjects
Amino Acid Sequence
Animals
brain
Brain - enzymology
Chromatography, High Pressure Liquid
Hydrolysis
peptidyl dipeptidase A
Peptidyl-Dipeptidase A - metabolism
Rats
substance P
Substance P - metabolism
HPLC
ACE
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Summary:Highly purified rat brain angiotensin-converting enzyme hydrolyzes substance P which contains a C-terminal amino acid with an amidated carboxyl group. The hydrolysis of substance P verified by amino-group fluorometry and by high-performance liquid chromatography is inhibited by captopril, but not by phosphoramidon. The presence of sodium chloride is essential for the hydrolysis. The analyses of cleavage products indicate that the enzyme hydrolyzes substance P between Phe7-Phe8 and Phe8-Gly9 by an endopeptidase action, followed by successive release of dipeptides by a dipeptidyl carboxypeptidase action.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(83)90586-7