[Electrophoretic properties of arylamidases from various cattle organs].
Agar electrophoresis was employed to study the homogeneity of arylamidase enzymes in the soluble fractions of liver, kidney, heart, spleen, brain, pancreas, and muscle homogenates and in serum. Enzymatic activity was determined in relation to the L-leucyl- and L-lysyl-p-nitroanilide chromogenic substrates. In all cases, electrophoresis made it possible to find at least two active zones with different electrophoretic mobility and with different activity in relation to the two substrates used.
D000626:Aminopeptidases / Q000378:metabolism*; D000818:Animals; D002417:Cattle / Q000378:metabolism*; D004587:Electrophoresis, Agar Gel; D007668:Kidney / Q000201:enzymology; D008099:Liver / Q000201:enzymology; D009132:Muscles / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology; D010179:Pancreas / Q000201:enzymology; D013154:Spleen / Q000201:enzymology
D000626:Aminopeptidases
Elektroforetické vlastnosti arylamidáz z niektorých orgánov hovädzieho dobytka