ISOLATION BY COVALENT AFFINITY CHROMATOGRAPHY OF PENICILLIN-BINDING COMPONENTS FROM MEMBRANES OF BACILLUS-SUBTILIS
ISOLATION BY COVALENT AFFINITY CHROMATOGRAPHY OF PENICILLIN-BINDING COMPONENTS FROM MEMBRANES OF BACILLUS-SUBTILIS
复制标题
DOI：
10.1073/pnas.69.12.3751
复制
发表时间：
1972-01-01
影响因子：
11.1
通讯作者：
STROMING.JL
中科院分区：
文献类型：
--
作者：
BLUMBERG, PM;STROMING.JL
An affinity chromatography technique was developed to isolate the five penicillin-binding components present inBacillus subtilismembranes. The proteins were solubilized by the detergent Nonidet P-40, bound covalently to penicillin-substituted Sepharose, and subsequently eluted from the matrix with neutral hydroxylamine, which cleaves the penicilloyl-enzyme bond. Penicillin binding-component V, the D-alanine carboxypeptidase, makes up 1% of the total membrane protein. A modification of the above procedure enabled this enzyme to be obtained from the membrane in pure form in a single step with 50% overall recovery of enzymatic activity.
