产气荚膜梭菌多核苷酸磷酸化酶在蛋白水解过程中，其受聚赖氨酸或聚鸟氨酸刺激的活性优先丧失。
The preferential loss of the polylysine- or polyornithine-stimulated activity of Clostridium perfringens polynucleotide phosphorylase during proteolysis.
作者信息
Fitt P S, Wille H
出版信息
Biochem J. 1969 May;112(4):489-95. doi: 10.1042/bj1120489.
Abstract
- An improved method for the purification of Clostridium perfringens polynucleotide phosphorylase (nucleoside diphosphate-polyribonucleotide nucleotidyltransferase, EC 2.7.7.8) is described. The product was stable and was highly stimulated by polylysine or polyornithine. 2. It migrated as a single enzyme during sucrose-density-gradient centrifugation, and no separation of polymerization and phosphorolytic activities was observed. 3. Trypsin digestion caused a rapid, preferential loss of the polylysine- or polyornithine-stimulated activity, which was prevented by low concentrations of polyornithine. 4. The protection by polyornithine was not specific. 5. It is concluded that charge effects on the clostridial polynucleotide phosphorylase itself are primarily responsible for the stimulation of this enzyme by polylysine or polyornithine.
摘要
- 本文描述了一种改进的产气荚膜梭菌多核苷酸磷酸化酶（核苷二磷酸 - 多聚核糖核苷酸核苷酸转移酶，EC 2.7.7.8）的纯化方法。该产物稳定，且受到多聚赖氨酸或多聚鸟氨酸的高度刺激。2. 在蔗糖密度梯度离心中，它作为单一酶迁移，未观察到聚合活性和磷酸解活性的分离。3. 胰蛋白酶消化导致多聚赖氨酸或多聚鸟氨酸刺激的活性迅速、优先丧失，低浓度的多聚鸟氨酸可防止这种情况。4. 多聚鸟氨酸的保护作用不具有特异性。5. 得出的结论是，对梭菌多核苷酸磷酸化酶本身的电荷效应主要是多聚赖氨酸或多聚鸟氨酸刺激该酶的原因。
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本文引用的文献
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Biochemistry. 1967 Jun;6(6):1818-27. doi: 10.1021/bi00858a033.
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