Minimal functional size of porcine lung and testicular angiotensin-converting enzymes deduced from radiation inactivation analysis. Interaction of two highly homologous domains in somatic isoenzyme.

Abstract:

:Domain structures of porcine lung and testicular angiotensin-converting enzymes (ACE) were studied by radiation inactivation to test the hypothesis that lung ACE has two catalytic sites localized to discrete, structurally independent domains (the N- and C-domains) of approximately equal size. The minimum functional sizes of lung and testicular ACE, calculated from the inactivation curves obtained, were 140 and 74 kDa, respectively. Since testicular ACE has been demonstrated to contain only the C domain, this result indicates that the two domains in lung ACE are not independent but are, in fact, structurally tightly linked.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Sakaguchi H,Hirose S,Kume T,Hagiwara H

doi

10.1016/0014-5793(92)80882-h

keywords:

subject

Has Abstract

pub_date

1992-06-29 00:00:00

pages

144-6

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(92)80882-H

journal_volume

305

pub_type

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