[Various properties of angiotensin-converting enzyme from the seal Phoca groenlandica].
It was found that the molecular mass of the angiotensin-converting enzyme from seal (Phoca groenlandica) lungs determined by electrophoresis in 7.5% PAAG in the presence of sodium dodecyl sulfate is 150 kD. The enzyme has a pH optimum with respect to hippuryl-L-histidyl-L-leucine at 7.3--7.5; KM is 1.2 mM. The enzyme is inhibited by the substrate to form a nonproductive ES2 complex with the dissociation constant (Ks') of 4.8 mM. The activation of the seal angiotensin-converting enzyme in the presence of NaCl was studied. The bradykinin-potentiating factor (SQ 20881) inhibits the seal enzyme with a high efficiency (IC50 = 2.5.10(-8) M). Monoclonal antibodies to the angiotensin-converting enzyme from human lungs do not interact with its seal lung counterpart, which points to the species specificity of the angiotensin-converting enzyme.
Sakharov
Iu I
IuI
Dukhanina
E A
EA
Danilov
S M
SM
Sakandelidze
O G
OG
D000806:Angiotensin-Converting Enzyme Inhibitors; D000818:Animals; D010872:Caniformia / Q000378:metabolism*; D007700:Kinetics; D008168:Lung / Q000201:enzymology*; D007703:Peptidyl-Dipeptidase A / Q000302:isolation & purification* / Q000378:metabolism; D046048:Seals, Earless / Q000378:metabolism*; D013379:Substrate Specificity
D000806:Angiotensin-Converting Enzyme Inhibitors; D007703:Peptidyl-Dipeptidase A
Issledovanie nekotorykh svoĭstv angiotenzinprevrashchaiushchego fermenta tiulenia Phoca groenlandica.