[Isolation and properties of bovine kidney aminopeptidase A].
Aminopeptidase A, which specifically hydrolyses N-terminal dicarbonic amino acid residues containing free alpha-amino groups, is isolated from bovine kidney. The enzyme is 500-fold purified and is homogenous under electrophoresis and ultracentrifugation. Aminopeptidase A has pH optimum of 7.5, it is activated with Ca2+ and inactivated with EDTA. Its molecular weight is 53000. The enzyme hydrolyses alpha-L-aspartyl-beta-naphtylamide and splits peptides having N-terminal glycine, lysine, arginine and alanine are hydrolyzed by the enzyme much slower. Aminopeptidase A does not attack alpha-L-alanyl-beta-naphtylamide, leucineamide, insulin, peptides with blocked N-terminal amino acid and peptides which have proline to be the second N-terminal amino acid.
D000626:Aminopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D001224:Aspartic Acid; D002118:Calcium / Q000494:pharmacology; D002417:Cattle; D004492:Edetic Acid / Q000494:pharmacology; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D007668:Kidney / Q000201:enzymology*; D013379:Substrate Specificity
D001224:Aspartic Acid; D004492:Edetic Acid; D000626:Aminopeptidases; D002118:Calcium
Vydelenie i svoistva aminopeptidazy A iz pochek byka.