| Literature DB >> 6381163 |
M Kouyoumdjian, D R Borges, J L Prado.
Abstract
A kinin-inactivating serine-endopeptidase from rat liver was purified to an activity of 912 mU/mg of protein, when measured on bradykinin. The endopeptidase molecular weight, estimated by gel filtration, was 68,000. Its isoelectric point was close to pH 4.9. Vm for the hydrolysis of bradykinin, was 1.25 mumol/min/mg protein; Km was 28 microM. The two hydrolysis products from bradykinin were the pentapeptide Arg1-Phe5 and the tetrapeptide Ser6-Arg9.Entities:
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Year: 1984 PMID： 6381163 DOI： 10.1016/0020-711x(84)90183-6
Source DB: PubMed Journal: Int J Biochem ISSN： 0020-711X