Partial purification and properties of a transamidinase from Lathyrus sativus seedlings. Involvement in homoarginine metabolism and amine interconversions.

A transamidinase was purified 463-fold from Lathyrus sativus seedlings by affinity chromatography on homoarginine--Sepharose. The enzyme exhibited a wide substrate specificity, and catalysed the reversible transfer of the amidino groups from donors such as arginine, homoarginine and canavanine to ac...

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Bibliographische Detailangaben
Hauptverfasser: Srivenugopal, K S, Adiga, P R
Format: Artigo
Sprache:Inglês
Veröffentlicht: 1980
Schlagworte:
Research Article
Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC1162036/
https://ncbi.nlm.nih.gov/pubmed/6163426
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