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Primary structure of aspartate aminotransferase from horse heart and comparison with that of other homotopic and heterotopic isoenzymes

Authors
Journal
Comparative Biochemistry and Physiology Part B Comparative Biochemistry
0305-0491
Publisher
Elsevier
Publication Date
Volume
76
Issue
3
Identifiers
DOI: 10.1016/0305-0491(83)90280-8
Disciplines
  • Biology

Abstract

Abstract 1. 1. Sulphydryl groups of mitochondrial aspartate aminotransferase from horse heart were titrated with 5,5′-dithiobis (2-nitrobenzoic acid). 2. 2. From analysis of peptic peptides, 378 amino acid residues (94.3% of the total) in the protein were identified. 3. 3. The results of amino acid sequence analysis are compared with those of cytosolic and mitochondrial aspartate aminotransferases from other sources.

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