Tissue distribution and characterization of prorenin-converting enzyme in mouse.

Abstract:

:Renin is produced from an inactive precursor, prorenin, through endoproteolytic cleavage at paired basic amino-acid residues. Using (35S)methionine-labeled prorenin, that was synthesized with Xenopus oocyte expression system, as a substrate, we have determined the tissue distribution and the nature of prorenin-converting activity in mouse. The highest activity was found in the submandibular gland of male ICR mouse. The activity of the enzyme seemed to be parallel to that of renin. This enzyme activity, with an optimal pH 8.0-8.5, was inhibited by leupeptin, antipain and benzamidine.

authors

Nakayama K,Kim WS,Hatsuzawa K,Hashiba K,Murakami K

doi

10.1016/s0006-291x(89)80057-9

subject

Has Abstract

pub_date

1989-01-31 00:00:00

pages

369-76

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(89)80057-9

journal_volume

158

pub_type

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