Isolation, charecterisation and possible mode of action of antiseminalplasin, a new protein that inhibits the antimicrobial activity of seminalplasmin

VEENA N RAO & P M BHARGAVA

Centre for Cellular and Molecular Biology, Hyderabad, India

Published in: Biochemical Journal, 1985, 227, 609-619.

Abstract:

The isolation from bovine seminal plasma and purification of a new protein called ‘antiseminalplasmin’, which reverses the inhibition of the growth of, and RNA synthesis in, Escherichia coli by seminalplasmin (another protein of bovine seminal plasma), is described. Antiseminalplasmin, a weakly acidic protein, has a minimum Mr of about 39 000 and appears to consist of three acidic peptide chains that move close to each other on electrophoresis on cellulose acetate strips or on sodium dodecyl sulphate/18%-(w/v)-polyacrylamide gels. Antiseminalplasmin has a tendency to oligomerize at slightly alkaline pH values; it does not bind to seminalplasmin or to DNA, and does not reverse the inhibition by seminalplasmin of transcription in vitro by purified E. coli RNA polymerase. It appears that antiseminalplasmin may act by binding to the cell surface and preventing the entry of seminalplasmin into the cells. By itself, antiseminalplasmin has no effect on the growth of E. coli.

PMID: 2408604

Keywords:
Chromatography, Gel Electrophoresis, Escherichia coli/drug effects, Escherichia coli/growth & development, Isoelectric Focusing, Peptide Hydrolases, Poly U/metabolism, Proteins/isolation & purification, Proteins/pharmacology, RNA/biosynthesis, Ribonuclease, Pancreatic/metabolism, Ribonucleases, Seminal Vesicle Secretory Proteins, Transcription, Genetic

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Isolation, charecterisation and possible mode of action of antiseminalplasin, a new protein that inhibits the antimicrobial activity of seminalplasmin. VEENA N RAO & P M BHARGAVA. Biochemical Journal, 1985, 227, 609-619.

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