刀豆氨酸化包膜蛋白与正常包膜蛋白的比较。
Comparison of canavanyl-envelope proteins to normal envelope proteins.
作者信息
Allen T D, Rogers P
出版信息
J Bacteriol. 1976 Jul;127(1):674-6. doi: 10.1128/jb.127.1.674-676.1976.
Abstract
Electrophoretic analysis showed arginine- and canavanine-containing envelope proteins to be qualitatively the same. Quantitative differences may be due to rapid degradation of some canavanine-containing envelope proteins.
摘要
电泳分析表明，含精氨酸和刀豆氨酸的包膜蛋白在性质上是相同的。数量上的差异可能是由于一些含刀豆氨酸的包膜蛋白快速降解所致。
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本文引用的文献
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A simple method for the isolation and purification of total lipides from animal tissues.一种从动物组织中分离和纯化总脂质的简单方法。
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Canavanine death in Escherichia coli.大肠杆菌中的刀豆氨酸致死现象。
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Mechanism of canavanine death in Escherichia coli. II. Membranes-bound canavanyl-protein and nuclear disruption.
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Properties of the growing point region in the bacterial chromosome.细菌染色体中生长点区域的特性
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Intracellular protein degradation in mammalian and bacterial cells.哺乳动物细胞和细菌细胞中的细胞内蛋白质降解
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