منابع مشابه
Anaerobic induction of alanine aminotransferase in barley root tissue.
Alanine aminotransferase, otherwise called glutamate-pyruvate aminotransferase (GPT), activity increases up to fourfold during several days of anaerobic induction in barley (Hordeum vulgare L.) roots, reaching a maximum activity of 13 international units per gram fresh weight. This increase in activity paralleled the increase in alcohol dehydrogenase activity in the same root tissue. Upon retur...
متن کاملAlanine aminotransferase controls seed dormancy in barley
Dormancy allows wild barley grains to survive dry summers in the Near East. After domestication, barley was selected for shorter dormancy periods. Here we isolate the major seed dormancy gene qsd1 from wild barley, which encodes an alanine aminotransferase (AlaAT). The seed dormancy gene is expressed specifically in the embryo. The AlaAT isoenzymes encoded by the long and short dormancy alleles...
متن کاملAlanine Aminotransferase
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....
متن کاملOptimization of methods for aspartate aminotransferase and alanine aminotransferase.
Conditions for accurate measurement of catalytic activity of aspartate aminotransferase and alanine aminotransferase in human serum have been reinvestigated. The basic variables (kind of buffer, buffer concentration, pH, ion effects, and the influence of pyridoxal-5-phosphate) can now be considered optimized. On this basis, the kinetic parameters of both aminotransferases were determined, i.e.,...
متن کاملAffinity 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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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1989
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.90.4.1305