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Aspartate aminotransferase isozymes from rabbit liver. Purification and properties.

Authors :
Kuramitsu S
Inoue K
Kondo K
Aki K
Kagamiyama H
Source :
Journal of biochemistry [J Biochem] 1985 May; Vol. 97 (5), pp. 1337-45.
Publication Year :
1985

Abstract

Cytosolic and mitochondrial isozymes of aspartate aminotransferase (L-aspartate:2-oxoglutarate aminotransferase [EC 2.6.1.1] ) were purified to homogeneity from rabbit liver. The rabbit liver isozymes were closely similar to the corresponding isozymes from other sources, including human heart, pig heart, chicken heart, and rat liver, in their molecular weights, absorption spectra, amino acid compositions, isoelectric points, and Michaelis constants for the substrates. The NH2-terminal amino acid sequences of rabbit liver isozymes were identified up to 30 residues, and showed some differences from those of the corresponding isozymes obtained from other animals so far studied.

Details

Language :
English
ISSN :
0021-924X
Volume :
97
Issue :
5
Database :
MEDLINE
Journal :
Journal of biochemistry
Publication Type :
Academic Journal
Accession number :
4030726
Full Text :
https://doi.org/10.1093/oxfordjournals.jbchem.a135186