title: 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.
authors.affiliation: Department of Biological Sciences, Tokyo Institute of Technology, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Sakaguchi
authors.forename: S
authors.initials: S
authors.lastname: Hirose
authors.forename: T
authors.initials: T
authors.lastname: Kume
authors.forename: H
authors.initials: H
authors.lastname: Hagiwara
mesh_terms: D000818:Animals; D001665:Binding Sites; D004307:Dose-Response Relationship, Radiation; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism / Q000528:radiation effects; D008168:Lung / Q000201:enzymology*; D008297:Male; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry / Q000378:metabolism* / Q000528:radiation effects; D013552:Swine; D013737:Testis / Q000201:enzymology*
chemical_list: D007527:Isoenzymes; D007703:Peptidyl-Dipeptidase A