Effect of polyelectrolytes on serine proteinase secretion by Bacillus subtilis.
Addition of polycations with molecular masses of 5-40 kDa as well as Na+, stimulated serine proteinase secretion by Bacillus subtilis cells. Polyanions and higher-molecular-mass polycations (100-200 kDa) were inefficient. The enzyme yields in the presence of polycations or Na+ were equal in magnitude. The results indicate that the cations, apparently counteracting the negative surface charge of the bacterial plasma membrane, cause the desorption of the serine (alkaline) proteinase. The synthesis of the proteinase is inferred to be stopped as the enzyme is bound to the outer surface of the plasma membrane. The desorption of the enzyme thus induces the synthesis of the new portions of proteinase.
Artemov
A V
AV
Department of Cell Physiology and Immunology, Moscow State University, USSR.
Samuilov
V D
VD
D001412:Bacillus subtilis / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology; D004573:Electrolytes / Q000494:pharmacology*; D011094:Polyethyleneimine / Q000494:pharmacology; D011107:Polylysine / Q000494:pharmacology; D012697:Serine Endopeptidases / Q000378:metabolism*; D012965:Sodium Chloride / Q000494:pharmacology
D004573:Electrolytes; D011107:Polylysine; D012965:Sodium Chloride; D011094:Polyethyleneimine; D012697:Serine Endopeptidases