Bacteriolytic activity of seminalplasmin.
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 Ca2+, Mn2+ and Mg2+ at millimolar concentrations. Maximum lysis of Escherichia coli was obtained at 37 degrees 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.
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001412:Bacillus subtilis / Q000187:drug effects; D001433:Bacteriolysis / Q000187:drug effects*; D004926:Escherichia coli / Q000187:drug effects; D007700:Kinetics; D011506:Proteins / Q000494:pharmacology*; D012329:RNA, Bacterial / Q000096:biosynthesis; D029607:Seminal Vesicle Secretory Proteins
D000900:Anti-Bacterial Agents; D011506:Proteins; D012329:RNA, Bacterial; D029607:Seminal Vesicle Secretory Proteins