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 posses the morphology and stability of native pahge fd. Furthermore, subtilisin proteolysis proved to be an efficient instrument in detecting variations in the topology of the g8p of related filamentous phages. Copyright © 1992, Wiley Blackwell. All rights reserved
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CITATION STYLE
SCHWIND, P., KRAMER, H., KREMSER, A., RAMSBERGER, U., & RASCHED, I. (1992). Subtilisin removes the surface layer of the phage fd coat. European Journal of Biochemistry, 210(2), 431–436. https://doi.org/10.1111/j.1432-1033.1992.tb17438.x
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