Abstract
The amino acid sequences of 39 tryptic peptides from carboxymethylated mitochondrial aspartate aminotransferase from pig heart muscle were analyzed. The peptides were purified by gel filtration, ion exchange column chromatography, paper chromatography, and high voltage paper electrophoresis, and their sequences were examined by manual Edman degradation, carboxypeptidase digestion, and fragmentation with thermolysin or chymotrypsin. These peptides accounted for 318 of the total 401 amino acid residues in the protein subunit.
Highlights
From the Department of Biochemistry, Shiga Unioersityof Medical Science, Ohtsu, Shiga 520-21Japan; the §Departmentof Pharmacology, Osaka Uniuersity Medical School, Kitaku, Osak5a30 Japan; and the YDepnrtmentof Biochemistry, Kumamoto University Medical School, Honjo, Kumamoto 860 Japan
The peptides were purified by gel filtration, ion exchange column chromatography, paper chromatography, and high voltage paper electrophoresis,andtheir sequences were examined by manual Edmadnegradation,carboxypeptidase digestion, and fragmentation with thermolysin or chymotrypsin.These peptides accountedfor 318 of the total 401 amino acid residues in the protein subunit
We animals, plants, and microorganisms. It is important in nitro- reported the complete amino acid sequence of m-AAT in a gen and carbon metabolism inthe cell, catalyzing the following preliminary communication [21] without giving details of exreaction: perimental procedures
Summary
The aminoacid sequences of 39 tryptic peptides from carboxymethylated mitochondrial aspartate aminotransferase from pig heart muscle were analyzed. The primary structureof the cytosolic isoenzyme from pig heart has been established by Ovchinnikov et al [18]and independently by Doonan et al [19]. We reported the partial aminoacid sequence of mitochondrialAATfrom pig heart muscle,including the sequence of the NHr-terminal 52 residues [13], 37 residues surrounding a specific lysine residue that forms an aldimine It is important in nitro- reported the complete amino acid sequence of m-AAT in a gen and carbon metabolism inthe cell, catalyzing the following preliminary communication [21] without giving details of exreaction: perimental procedures. In this series of three papers,we report studiesestablishing the complete sequence of m-AAT.
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