The Primary Structure of Mitochondrial Aspartate Aminotransferase from Human Heart

Overview

Journal Biochim Biophys Acta

Specialties Biochemistry
Biophysics

Date 1985 Nov 8

PMID 4052435

Citations 5

Authors

F Martini

S Angelaccio

D Barra

S Pascarella

B Maras

S Doonan

F Bossa

Affiliations

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Abstract

The complete amino acid sequence of the mitochondrial aspartate aminotransferase (L-aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1) from human heart has been determined based mainly on analysis of peptides obtained by digestion with trypsin and by chemical cleavage with cyanogen bromide. Comparison of the sequence with those of the isotopic isoenzymes from pig, rat and chicken showed 27, 29 and 55 differences, respectively, out of a total of 401 amino acid residues. Evidence for structural microheterogeneity at position 317 has also been obtained.

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