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Subtilisin removes the surface layer of the phage fd coat.

Authors :
Schwind, Peter
Kramer, Hansgerd
Kremser, Andreas
Ramsberger, Uwe
Rasched, Ihab
Source :
European Journal of Biochemistry. 12/1/92, Vol. 210 Issue 2, p431-436. 6p.
Publication Year :
1992

Abstract

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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00142956
Volume :
210
Issue :
2
Database :
Academic Search Index
Journal :
European Journal of Biochemistry
Publication Type :
Academic Journal
Accession number :
13714072
Full Text :
https://doi.org/10.1111/j.1432-1033.1992.tb17438.x