C 组链球菌噬菌体相关溶素的纯化及物理性质
Purification and physical properties of group C streptococcal phage-associated lysin.
作者信息
Fischetti V A, Gotschlich E C, Bernheimer A W
出版信息
J Exp Med. 1971 May 1;133(5):1105-17. doi: 10.1084/jem.133.5.1105.
Abstract
A purification procedure for the Group C phage-associated lysin is described utilizing tetrathionate to protect the enzyme's -SH group(s) from thiol-inactivating agents. A 652-fold purification has been accomplished yielding a solution in which the enzyme activity corresponds to essentially a single band on polyacrylamide gel which accounts for 70% of the total protein in the preparation. A molecular weight of 101,000 and frictional ratio of 1.526 was determined for the lysin utilizing experimentally determined values for its Stokes radius and sedimentation coefficient.
摘要
描述了一种用于C组噬菌体相关溶素的纯化程序，该程序利用连四硫酸盐保护酶的巯基免受硫醇失活剂的影响。已实现652倍的纯化，得到一种溶液，其中酶活性在聚丙烯酰胺凝胶上基本对应于一条带，该带占制剂中总蛋白的70%。利用其实验测定的斯托克斯半径和沉降系数值，确定了溶素的分子量为101,000，摩擦比为1.526。
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