[Chemical and physicochemical properties of the H antigen (flagellin) isolated from Salmonella abortus ovis].
Some chemical and physiochemical properties of H-antigen, obtained through immunoabsorption, were studied. By applying the method of Davis, during a disc electrophoresis in a polyacrylic amide gel, it was proved that the molecule of flagellin is homogenous and is built up of only one polypeptic chain. On the other hand, by applying Weber's and Osborn's method, it was proved that flagellin is a protein having a molecular weight of about 53000 daltons. It showed its isoelectric point at pH 5.2, proved through Heil's and Zillig's method on strips of acetate cellulose (cellogel). The investigated aminoacidic composition showed the presence of 15 aminoacids wtih an approximative succession and a relative quantity of the separate aminoacids common to the flagellins of the different representatives of the genus Salmonella. No presence of cysteine, tryptophan, methionine and sigma-N-methylated lysin, were proved.
D000596:Amino Acids / Q000032:analysis; D000942:Antigens, Bacterial / Q000032:analysis* / Q000302:isolation & purification; D001426:Bacterial Proteins / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D002627:Chemistry, Physical; D005408:Flagellin / Q000032:analysis* / Q000302:isolation & purification; D007526:Isoelectric Point; D008970:Molecular Weight; D012475:Salmonella / Q000276:immunology*
D000596:Amino Acids; D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D005408:Flagellin
Niakoi khimichni i fizikokhimichni svoístva na H-antigen (flagelin), izoliran ot Salmonella abortus ovis.