Amino acid composition and terminal residues of aspartate aminotransferase from ox heart

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Amino acid composition and terminal residues of aspartate aminotransferase from ox heart.

1. The amino acid composition of highly purified aspartate aminotransferase from ox heart was determined. 2. Alanine is the only N-terminal residue. 3. Leucine was identified as the only C-terminal residue. 4. No disulphide bridges are present in the enzyme molecule. 5. The thiol groups are not equally accessible, the accessibility being comparatively easier in the apoenzyme molecule.

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Aspartate: 2-oxoglutarate aminotransferase from trichomonas vaginalis. Identity of aspartate aminotransferase and aromatic amino acid aminotransferase.

Aspartate: 2-oxoglutarate aminotransferase from the anaerobic protozoon Trichomonas vaginalis was purified to homogeneity and characterized. It is a dimeric protein of overall Mr approx. 100000. Only a single isoenzyme was found in T. vaginalis. The overall molecular and catalytic properties have features in common with both the vertebrate cytoplasmic and mitochondrial isoenzymes. The purified ...

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Complete amino acid sequence of mitochondrial aspartate aminotransferase from pig heart muscle. Tryptic peptides.

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 fragmenta...

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N-Terminal Amino Acid Residues of Gelatin

Levvy, G. A. (1948). Biochem. J. 42, 2. Levvy, G. A. (1952). Biochem. J. 52, 464. Levvy, G. A. (1954). Biochem. J. 58, 462. Levvy, G. A. & Marsh, C. A. (1952). Biochem. J. 52, 690. Lohmar, R., Dimler, R. J., Moore, S. & Link, K. P. (1942). J. biol. Chem. 143, 551. Marsh, C. A. (1952). J. chem. Soc. p. 1578. Marsh, C. A. (1954). Biochem. J. 58, 609. Marsh, C. A., Alexander, F. & Levvy, G. A. (19...

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Amino acid composition and amino-terminal sequence of yeast enolase.

The recent finding (1, 2) that part of the enolase molecule can be removed by digestion with leucine aminopeptidase or carboxypeptidase without change in enzymic activity has prompted a detailed study of the relation between structure and activity in this enzyme. As a basis for such investigations it is necessary to have a knowledge of the principal features of enolase structure; the amino acid...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1966

ISSN: 0006-2936

DOI: 10.1042/bj0990595