Open Accessl ‐Glutamate‐Phenylpyruvate Aminotransferase
Author(s) -
Scandurra R.,
Cannella C.,
Ferretti M. G.
Publication year - 1967
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1967.tb19519.x
Subject(s) - sephadex , fractionation , chromatography , enzyme , chemistry , lysis , size exclusion chromatography , ammonium , biochemistry , dissociation (chemistry) , organic chemistry
l ‐glutamate‐phenylpyruvate aminotransferase was extracted from beef kidney mitochondria. The purification procedure included lysis of mitochondria in n ‐butanol, ammonium sulphate fractionation between 55% and 80% saturation, gel filtration on G‐100 Sephadex and fractionation on DEAE‐Sephadex. The optimum pH of the enzyme is around 8. The enzyme is homogeneous to starch gel electrophoresis at various pH but shows two components when submitted to ultracentrifugal analyses. A possible dissociation of the enzyme into subunits dependent on concentration is discussed.