Separation of rat muscle aminopeptidases.
By means of chromatography on DEAE-Sephadex, two arylamidases (hydrolysing L-arginine 2-naphthylamide) and three dipeptidyl peptidases (hydrolysing dipeptide 2-naphthylamides) were distinguished in extracts of rat muscle. However, the arylamidase from the larger peak also hydrolysed the dipeptide 2-naphthylamides. Glycyl-L-arginine amide, an alternative substrate for dipeptidyl peptidase I, was not hydrolysed by arylamidase. L-Leucine amide was hydrolysed by an enzyme, presumed to be leucine aminopeptidase, from a separate peak, but was also hydrolysed by arylamidase. Arylamidase, dipeptidyl peptidase III and most of the leucine aminopeptidase could be extracted from the muscle with a neutral salt solution, but dipeptidyl peptidase I was extracted only in the presence of Triton X-100; dipeptidyl peptidase II showed an intermediate extraction behaviour.
D000626:Aminopeptidases / Q000302:isolation & purification*; D000818:Animals; D002403:Cathepsins / Q000032:analysis / Q000302:isolation & purification; D003593:Cytoplasm / Q000201:enzymology; D005260:Female; D007527:Isoenzymes / Q000302:isolation & purification; D007931:Leucyl Aminopeptidase / Q000302:isolation & purification; D008297:Male; D009132:Muscles / Q000201:enzymology*; D051381:Rats
D007527:Isoenzymes; D002403:Cathepsins; D000626:Aminopeptidases; D007931:Leucyl Aminopeptidase