Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
C-Terminal Identification of AD74, a Proteolytic Product of Enterococcus faecalis Aggregation Substance : Application of Liquid Chromatography/Mass Spectrometry
Jiro NAKAYAMAHiroshi WATARAIAkira ISOGAIDon B.CLEWELLAkinori SUZUKI
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1992 Volume 56 Issue 1 Pages 127-131

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Abstract

Sexual aggregation involved in conjugative transfer of Enterococcus faecalis plasmid pAD1 is enhanced by the sex pheromone cAD1, which is excreted from recipient cells. A membrane-anchored 137kDa protein is a pAD1-encoded aggregation substance designated asal, which is responsible for cell-cell contact and leads to the aggregation of cells. An AD74 protein is a proteolytic product corresponding to the N-terminal half of asal. The C-terminal of AD74 was identified as lysine at position 510 (K-510) by liquid chromatography/mass spectrometry (LC/MS) : it indicates that asal is cleaved specifically between K-510 and G-511.

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