[Polymorphism of water-soluble and triton-X 100-extractable esterases and proteins from Leptospira].
Electrophoresis in gel from polyacrylamide was used to study the water-soluble intracellular esterases, triton-X 100-extracted and proteins of three saprophytic and three pathogenic strains of leptospirae belonging to different serological types. The results of investigation of a relative mobility of 27 fractions with an esterasic activity and the molecular weight of eight of them showed that their polymorphism was mainly consecuent of structural differences. In examination of proteins extracted from the cell residues with triton-X 100 there was also revealed an intertype polymorphism: by acrylamide electrophoresis with sodium dodecylsulphate they were divided into 3--10 fractions with a molecular weight of from 20000 to 200000. The results of these studies are discussed as a manifestation of biochemical individuality of leptospirae of individual serological types.
D001426:Bacterial Proteins / Q000032:analysis* / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D004950:Esterases / Q000032:analysis* / Q000302:isolation & purification; D007919:Leptospira / Q000032:analysis* / Q000201:enzymology; D008970:Molecular Weight; D011092:Polyethylene Glycols; D011110:Polymorphism, Genetic
D001426:Bacterial Proteins; D011092:Polyethylene Glycols; D004950:Esterases
Polimorfizm vodorastvorimykh i ékstragirovannykh tritonom-X 100 ésteraz i proteinov iz leptospir