Affinity labeling of alanine aminotransferase by 3-chloro-L-alanine.

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Affinity labeling of alanine aminotransferase by 3-chloro-L-alanine.

The pyridoxal form of alanine aminotransferase from pig heart catalyzes the a,/? elimination reaction with 3chloro-L-alanine as the substrate to form equimolar amounts of pyruvate, ammonia, and chloride. The maximum rate of the a,/3 elimination reaction was 2.5 pmol/min/mg at pH 7.0 (25”(Z), approximately 0.5% that of the transamination reaction between L-alanine and 2-oxoglutarate. Time-depend...

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The pyridoxal form of alanine aminotransferase from pig heart catalyzes the a,/? elimination reaction with 3chloro-L-alanine as the substrate to form equimolar amounts of pyruvate, ammonia, and chloride. The maximum rate of the a,/3 elimination reaction was 2.5 pmol/min/mg at pH 7.0 (25”(Z), approximately 0.5% that of the transamination reaction between L-alanine and 2-oxoglutarate. Time-depend...

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An examination of the subcellular distribution of alanine aminotransferase activity in pig cardiac tissue showed that about 10% of the total activity was bound to particulate material, with the highest specific activity in the sarcosomal fraction. The soluble enzyme was obtained in a high state of purity, as indicated by sedimentation velocity, starch gel electrophoresis, and spectral analyses....

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1979

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(17)37915-2