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首页> 外文期刊>Journal of bacteriology >A mutation altering some properties of the neutral phosphatase in Chlamydomonas reinhardi: possible post-translational modification of phosphatase structure.
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A mutation altering some properties of the neutral phosphatase in Chlamydomonas reinhardi: possible post-translational modification of phosphatase structure.

机译:改变衣藻衣藻中性磷酸酶某些特性的突变:可能是磷酸酶结构的翻译后修饰。

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摘要

A mutant (PDs-) of Chlamydomonas reinhardi has been isolated which produces an altered neutral phosphatase. The wild-type (PDs+) and mutant (PDs-) phosphatases markedly differed in their thermosensitivities and electrophoretic mobilities. The heterozygous PDs-/PDs+ diploids produced only the wild-type electrophoretic form of the phosphatase. Mixing extracts of PDs- with extracts of various other strains in vitro resulted in the rapid transformation of the PDs- enzymic form into an enzymic variety, the properties (heat sensitivity, electrophoretic mobility) of which were similar to those of the wild-type neutral phosphatase. The results are discussed in relation to the idea that the PDs mutation is located not in the structural gene but rather in a modifying gene acting at the post-translational level.
机译:已经分离出莱茵衣藻的突变体(PDs-),其产生改变的中性磷酸酶。野生型(PDs +)和突变型(PDs-)磷酸酶的热敏性和电泳迁移率明显不同。杂合的PDs- / PDs +二倍体仅产生磷酸酶的野生型电泳形式。将PDs-的提取物与多种其他菌株的提取物在体外混合,导致PDs-酶形式快速转化为酶变种,其性质(热敏性,电泳迁移率)与野生型中性相似磷酸酶。关于PDs突变不在结构基因中而是在翻译后水平起作用的修饰基因中的想法进行了讨论。

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