PURIFICATION AND PROPERTIES OF ASPARTATE AMINO TRANSFERASE (E.C2.6.1.1) FROM SKELETEL MUSCLE OF DIRRHINA MRIGALA
PURIFICATION AND PROPERTIES OF ASPARTATE AMINO TRANSFERASE (E.C2.6.1.1) FROM SKELETEL MUSCLE OF DIRRHINA MRIGALA
Date
1980
Authors
CHHATBAR, S. K
VELANKAR, N. K
Journal Title
Journal ISSN
Volume Title
Publisher
Society of Fisheries Technologists (India) Cochin
Abstract
Aspartate aminotransferase (E. C. 2.6.1.1.) from the skeletal muscle of fresh water fish
Cirrhina mrigala has been purified 40 fold by ammonium sulphate fractionation, adsorption
on alumina Cs gel and chromatography using DEAE-cellulose column and the
properties of the purified enzyme studied. The pH optimum of the enzyme is 7.8. The
Km value of aspartic acid and 2-oxoglutaric acid are found to be 2.8 x 10- 3 M and
1.0 x 10-4 M respectively. The activity of enzyme is inhibited by p-chloromercurybenzoate,
hydroxylamine hydrochloride and sodium cyanide. The inhibition by pchloromercurybenzoate
is reversed by reduced glutathione, B-mercaptoethanol
and cysteine. Dicarboxylic acids such as maleic acid, malic acid and succinic
acid inhibit the enzyme activity. The enzyme is not activated by any of the metal
ions tested and heavy metal ions such as mercury and silver strongly inhibit the enzyme
activity
Description
Keywords
PURIFICATION, PROPERTIES ,ASPARTATE AMINO TRANSFERASE (E.C2.6.1.1) ,SKELETEL MUSCLE ,DIRRHINA MRIGALA
Citation
Fishery Tech 17(1):43-49