Abstract
The different transaminase reactions for 22 protein amino acids were investigated in extracts of cotyledons and growing tissues of 8-day-old bushbean seedlings when either α-ketoglutarate, oxaloacetate, pyruvate, or glyoxylate was used as amino group acceptor. The results indicate that both cotyledons and growing tissues exhibited a similar pattern of transaminase activities with respect to the amino acids normally required for protein synthesis. It was found that with the exception of proline, hydroxyproline, and cystine which did not appear to be transaminated, and of serine and threonine which were transaminated only when pyruvate or glyoxylate was provided as the amino group acceptor, all the other 17 amino acids were transaminated to different extents when each of the four keto acids tested was supplied as the amino group acceptor. Glutamic acid, aspartic acid, and alanine were, by far, the best amino group donors and α-ketoglutarate was generally found to be the best amino acceptor. Consideration is given to the number and substrate specificity of the aminotransferases catalyzing the reactions demonstrated in this study.
Publisher
Canadian Science Publishing
Cited by
15 articles.
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