SUBTILISIN REMOVES THE SURFACE-LAYER OF THE PHAGE-FD COAT

被引:26
作者
SCHWIND, P
KRAMER, H
KREMSER, A
RAMSBERGER, U
RASCHED, I
机构
[1] UNIV CONSTANCE,FAK BIOL,POSTFACH 5560,W-7750 CONSTANCE,GERMANY
[2] UNIV CONSTANCE,FAK PHYS,W-7750 CONSTANCE,GERMANY
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 210卷 / 02期
关键词
D O I
10.1111/j.1432-1033.1992.tb17438.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The major coat protein of native filamentous phage fd is vulnerable to digestion by subtilisin, but not by any of a number of other proteolytic enzymes. Degradation by the non-specific protease subtilisin occurs at specific sites in the N-terminal portion of g8p. The N-terminal part of the protein is considered to be the outer layer of a two-layered coat. Thus, subtilisin treatment results in a monolayered phage particle. These particles possess the morphology and stability of native phage fd. Furthermore, subtilisin proteolysis proved to be an efficient instrument in detecting variations in the topology of the g8p of related filamentous phages.
引用
收藏
页码:431 / 436
页数:6
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