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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1983-2-14
pubmed:abstractText
Biochemical fluorometric methods were used to investigate aminopeptidase A (APA; E.C.3.4.11.7) in the rat kidney homogenate and glomeruli and to compare it with aminopeptidase M (APM; E.C.3.4.11.2). It is shown that APA is a calcium-ion-dependent enzyme, while APM is not. To clarify the functional importance of APA and APM in the kidney, their activities were measured under the influence of angiotensins. Fluorimetric measurements in renal homogenate (with 2-naphthylamide derivatives as substrates), which represents mixed-enzyme tissue preparations containing a variety of peptidases besides APA and APM, showed a Km of 0.13 mM for APA and competitive inhibition of ANG II (K1 = 0.015 mM), and a Km of 0.24 for APM and competitive inhibition by ANG III (K1 = 0.003 mM). The remaining two angiotensins showed non-competitive inhibition of APA (ANG I, III) and APM (ANG I, II) in this preparation. For comparison purposes, fluorometric measurements were performed in microdissected glomeruli which contain only APA. A Km of 0.23 mM for the APA and a competitive inhibition of APA by ANG I and II were determined. Thus it was possible to show biochemically that APA is equivalent to angiotensinase A and that both APA and APM participate in angiotensin degradation in the kidney. APA initiating the breakdown of ANG I and II, and APM possibly continuing it in sequential fashion.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0301-5564
pubmed:author
pubmed:issnType
Print
pubmed:volume
74
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
247-61
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Aminopeptidase A is angiotensinase A. II. Biochemical studies on aminopeptidase A and M in rat kidney homogenate.
pubmed:publicationType
Journal Article, Comparative Study