Bacteriolytic activity of seminalplasmin

• Published in: Journal of general microbiology Vol. 133; no. 5; pp. 1265 - 1271
• Main Authors: Chitnis, S.N, Prasad, K.S.N, Bhargava, P.M
• Format: Journal Article
• Language: English
• Published: London Soc General Microbiol 01.05.1987; New York, NY Cambridge University Press
• Subjects: Action of physical and chemical agents on bacteria; animal proteins; Anti-Bacterial Agents - pharmacology; antibacterial properties; Bacillus subtilis - drug effects; Bacteriology; Bacteriolysis - drug effects; Biological and medical sciences; cattle; Escherichia coli - drug effects; Fundamental and applied biological sciences. Psychology; Kinetics; Microbiology; Proteins - pharmacology; RNA, Bacterial - biosynthesis; seminal plasma; Seminal Vesicle Secretory Proteins; Culture medium; Bovine; Drug susceptibility test; Escherichia coli; Autolysin; Antimicrobial agent; Plasmin; Dose activity relation; Proteins; Vertebrata; Mammalia; Lysis; Bacteria; Artiodactyla; Biological effect; Escherichieae; Ungulata; Enterobacteriaceae
• ISSN: 0022-1287; 1350-0872; 1465-2080
• DOI: 10.1099/00221287-133-5-1265

Centre for Cellular and Molecular Biology, Hyderabad 500007, India ABSTRACT SUMMARY: Seminalplasmin, an antimicrobial protein from bovine seminal plasma, lysed both Gram-positive and Gram-negative bacteria but not Candida albicans. The lytic activity was not lysozyme-like and was not affected by inhibitors of RNA or protein synthesis or by azide; it was strongly inhibited by divalent cations like Ca 2+ , Mn 2+ and Mg 2+ at millimolar concentrations. Maximum lysis of Escherichia coli was obtained at 37°C; heat treatment of E. coli drastically reduced its susceptibility to lysis by seminalplasmin. E. coli cells in the stationary phase of growth were lysed much less than those in the exponential phase, and those grown in an enriched medium were lysed much more than those grown in a minimal medium. It appears that the lytic activity of seminalplasmin is due to the activation of an autolysin.