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PURIFICATION AND PROPERTIES OF PANTETHEINASE FROM PIG KIDNEY
Author(s) -
CALVIÑO JOSÉ A.,
BARCIA RAMIRO
Publication year - 2002
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.2002.tb00868.x
Subject(s) - sephadex , chemistry , chromatography , cysteamine , fractionation , hydrolysis , enzyme , ammonium , specific activity , butanol , ammonium sulfate , biochemistry , ethanol , organic chemistry
Pantetheinase hydrolyzes specifically one of the carboamide linkages in pantetheine, leading to the formation of pantothenate and cysteamine. The enzyme from pig kidney cortex was purified to homogeneity as determined by SDS electrophoresis. Pantetheinase was solubilized by treatment with 1‐butanol, and then purified by thermal treatment, fractionation with ammonium sulfate and chromatography on CM‐Sephadex and DEAE‐Sephadex. The molecular weight of the purified pantetheinase was 72 kDa. No significant differences were found between the mercaptide and cysteamine methods for determination of the kinetic constants of the pantetheinase. The enzyme had a pH optimum of 9.0 and it was inhibited by pantethine and by oxidized glutation.