[Purification and partial characterization of an extracellular aminopeptidase of a collagenolytic bacterium: Empedobacter collagenolyticum].
An aminopeptidase was purified from the culture filtrates of a collagenolytic bacterium Empedobacter collagenolyticum. Purification of this enzyme was accomplished by ammonium sulphate precipitation, gel filtration on Sephadex-G200 and chromatography on DEAE-Sephacel. The purified enzyme seemed homogeneous on polyacrylamide gel electrophoresis. The molecular weight of the enzyme was about 100,000 daltons as determined by gel filtration on Sephadex-G200 but it was only 33,000 daltons by disc gel electrophoresis in the presence of sodium dodecyl sulphate. This enzyme selectively hydrolysed N-terminal arginine and lysine residues of peptides and arylamides substrates. The enzyme was strongly inhibited by EDTA, ZnCl2 and L-arginine.
D000577:Amides / Q000378:metabolism; D000626:Aminopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D001120:Arginine / Q000378:metabolism; D001419:Bacteria / Q000201:enzymology*; D003094:Collagen / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008239:Lysine / Q000378:metabolism; D008970:Molecular Weight; D010455:Peptides / Q000378:metabolism
D000577:Amides; D010455:Peptides; D003094:Collagen; D001120:Arginine; D000626:Aminopeptidases; D008239:Lysine
Purification et caractérisation partielle d'une aminopeptidase extracellulaire d'une bactérie collagénolytique: Empedobacter collagenolyticum.