莱茵衣藻L-天冬酰胺酶的分离与鉴定
Isolation and characterization of a Chlamydomonas L-asparaginase.
作者信息
Paul J H
出版信息
Biochem J. 1982 Apr 1;203(1):109-15. doi: 10.1042/bj2030109.
Abstract
An L-asparaginase (EC 3.5.1.1) specific for L-asparagine has been purified from a marine Chlamydomonas species, the first such enzyme to be purified from a microalga. The purified enzyme (mol.wt. 275 000) possessed a Km for asparagine of 1.34 x 10(-4) M and showed limited antitumour activity in an antilymphoma assay in vivo. Properties of the enzyme are contrasted with those of asparaginases from prokaryotic and eukaryotic sources.
摘要
一种对L-天冬酰胺具有特异性的L-天冬酰胺酶（EC 3.5.1.1）已从一种海洋衣藻中纯化出来，这是首次从微藻中纯化出此类酶。纯化后的酶（分子量275000）对天冬酰胺的Km值为1.34×10⁻⁴ M，并且在体内抗淋巴瘤试验中显示出有限的抗肿瘤活性。该酶的特性与来自原核和真核生物来源的天冬酰胺酶的特性形成对比。
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