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The purification and some properties of a stereospecific D-asparaginase from an extremely thermophilic bacterium, Thermus aquaticus.

A specific D-asparaginase was isolated and crystallized from Thermus aquaticus strain T351. It is present in larger amounts than the L-asparaginase. The enzyme has a molecular weight of 60 000, an isoelectric point of 4.8 and a Km of 2 mM. It has 6 disulphide bonds/molecule, and a histidine residue...

詳細記述

保存先:
書誌詳細
主要な著者: Guy, G R, Daniel, R M
フォーマット: Artigo
言語:Inglês
出版事項: 1982
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC1158297/
https://ncbi.nlm.nih.gov/pubmed/7115316
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