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Purification and Characterization of Aminopeptidase from Chicken Intestine
Author(s) -
Jamadar V.K.,
Jamdar S.N.,
Dandekar S.P.,
Harikumar P.
Publication year - 2003
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2003.tb05691.x
Subject(s) - aminopeptidase , enzyme , size exclusion chromatography , puromycin , biochemistry , leucyl aminopeptidase , chemistry , substrate specificity , substrate (aquarium) , ion chromatography , dipeptidase , affinity chromatography , chromatography , biology , amino acid , leucine , protein biosynthesis , ecology
An aminopeptidase was purified 839‐fold with 15% recovery from chicken intestine by a procedure involving ion exchange, gel filtration, hydrophobic interaction and affinity chromatography. The enzyme is a heteridimer of subunits 94000 Da and 66000 Da. The substrate specificity of the enzyme was in the order ala > arg > leu‐β‐naphthylamide. The enzyme was strongly inhibited by bestatin, puromycin, and 1, 10‐phenanthroline. The aminopeptidase showed maximum activity at pH 6 and 40 to 50 °C. The enzyme significantly differs from the hitherto known major classes of aminopeptidases from chicken tissues in terms of molecular weight and biochemical characteristics.