从肺炎链球菌中纯化青霉素结合蛋白3
Purification of penicillin-binding protein 3 from Streptococcus pneumoniae.
作者信息
Hakenbeck R, Kohiyama M
出版信息
Eur J Biochem. 1982 Oct;127(2):231-6. doi: 10.1111/j.1432-1033.1982.tb06860.x.
Abstract
Penicillin-binding protein 3 from wild-type Streptococcus pneumoniae has been purified to homogeneity by solubilization with Triton X-100 and successive column chromatography. The penicillin-binding activity during the fractionation procedure was monitored with a rapid filter binding assay using [3H]propionylampicillin and penicillin-binding protein 3 identified after fluorography of dodecyl sulfate gels. The purified protein showed penicillin-sensitive D,D-carboxypeptidase activity.
摘要
通过用 Triton X-100 增溶并连续进行柱色谱法，已将野生型肺炎链球菌的青霉素结合蛋白 3 纯化至同质。在分级分离过程中，使用 [3H]丙酰氨苄青霉素通过快速滤膜结合测定法监测青霉素结合活性，并在十二烷基硫酸盐凝胶的荧光显影后鉴定青霉素结合蛋白 3。纯化后的蛋白显示出对青霉素敏感的 D,D-羧肽酶活性。
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