Title: | "C-terminal identification of AD74, a proteolytic product of Enterococcus faecalis aggregation substance: application of liquid chromatography/mass spectrometry" |
Author(s): | Nakayama J; Watarai H; Isogai A; Clewell DB; Suzuki A; |
Address: | "Department of Agricultural Chemistry, University of Tokyo, Japan" |
Journal Title: | Biosci Biotechnol Biochem |
ISSN/ISBN: | 0916-8451 (Print) 0916-8451 (Linking) |
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 137 kDa 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" |
Keywords: | "Amino Acid Sequence Bacterial Proteins/chemistry/genetics *Cell Adhesion Molecules Cell Aggregation Chromatography, High Pressure Liquid Enterococcus faecalis/*chemistry/genetics Mass Spectrometry Molecular Sequence Data Peptide Fragments/chemistry Peptid;" |
Notes: | "MedlineNakayama, J Watarai, H Isogai, A Clewell, D B Suzuki, A eng Research Support, Non-U.S. Gov't England 1992/01/01 Biosci Biotechnol Biochem. 1992 Jan; 56(1):127-31. doi: 10.1271/bbb.56.127" |