Release of a plasma membrane-bound triaminopeptidase activity from mammalian cells by thermolysin.

T Aoyagi,H Suda,M Nagai,H Tobe,J Suzuki,T Takeuchi,H Umezawa

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS（1978）

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摘要

Aminopeptidase and other enzyme activities on cellular surface were determined in the presence and absence of endopeptidases. Gly-Pro-Leu-AP activity was specifically released into the medium by thermolysin treatment, while the other activities retained on the cellular surface were markedly decreased. A similar phenomenon was also observed in rat liver membrane, mouse FM3A, spleen lymphocyte and other cells. Structural rearrangement of some protein components in the cell plasma membrane was suggested.

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关键词

ap-a,tyr-ap,β-na,leu-ap,aminopeptidase a,gly-pro-leu-ap,methionine aminopeptidase,ala-ap,alanine aminopeptidase,thyrosine aminopeptidase,3yl,leucine aminopeptidase,phe-ap,phenylalanine aminopeptidase,glycyl-proline aminopeptidase,glycyl-prolylleucine aminopeptidase,fisher rat embryo,met-ap,established from embrionic kidney of mouse strain c3h,ap-b,gly-pro-ap,aminopeptidase b,β-naphthylamide c3h2k

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