Characterization of insulinase from mammalian and non-mammalian livers.
The Michaelis constants (Km's) and maximum reaction velocities (Vmax's) for the degradation of beef insulin by livers from frogs, guinea pigs, rats, a rabbit, a dog and a pig were determined. The Km's for mammalian livers appear to be species-dependent and range from 0.25 microM to 0.65 microM. The Km for frog liver was somewhat lower, averaging 0.13 microM. The Km is independent of animal age, but the enzyme concentrations (Vmax) were greatly reduced in the fetal guinea pig and 3 day rat compared to the adult livers. There appears to be no relation between Km and the chemical dissimilarity between beef insulin and endogenous insulin of the species, since guinea pig liver insulinase had a Km (0.50 microM) intermediate between dog (0.47 microM) and pig (0.65 microM) liver insulinase although guinea pig insulin has a markedly different amino acid sequence and biologic activity.
D000375:Aging; D000818:Animals; D001001:Anura; D004285:Dogs; D006168:Guinea Pigs; D007339:Insulysin / Q000302:isolation & purification*; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D011817:Rabbits; D051381:Rats; D013045:Species Specificity; D013552:Swine
D010447:Peptide Hydrolases; D007339:Insulysin