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食用蛙肝脏酸性磷酸酶的多种形式的分离及部分特性研究

Acid phosphatase from liver of the frog Rana esculenta, separation and partial characterization of multiple forms.

作者信息

Kubicz A, Dratewka E, Malicka-Błaszkiewicz M

出版信息

Acta Biochim Pol. 1978;25(4):349-59.

PMID:35912
Abstract
  1. Acid phosphatase (AcPase) from liver of the frog, Rana esculenta has been isolated and purified. The enzyme is heterogeneous, showing 4 activity zones on disc electrophoresis. The AcPase was separated into 3 peaks on DEAE-cellulose. Peak A corresponding to the electrophoretic AcPase IV represents an extensively purified enzyme form. 2. The separated enzyme forms are change isomers with a molecular weight of about 33,000. They differ markedly in substrate requirements and sensitivity towards activators and inhibitors. All of them are highly activated by dithiothreitol, show a rather restricted substrate specificity, and marked activity against ATP.
摘要
  1. 已从食用蛙肝脏中分离并纯化出酸性磷酸酶(AcPase)。该酶具有异质性,在圆盘电泳上显示出4个活性区。AcPase在DEAE-纤维素上分离为3个峰。对应于电泳AcPase IV的峰A代表一种高度纯化的酶形式。2. 分离出的酶形式是分子量约为33,000的变构异构体。它们在底物需求以及对激活剂和抑制剂的敏感性方面有显著差异。所有这些酶都被二硫苏糖醇高度激活,底物特异性相当有限,并且对ATP有显著活性。

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