02354nas a2200301   4500000000100000008004100001260001300042653001200055653002600067653002400093653001500117653002300132653004000155653001300195653001800208653001100226653001200237653002500249653001400274100002000288700001400308700001600322245013800338300001100476490000700487520154400494022001402038       1982                            d  c1982 Sep10aAnimals10aAntibodies, Bacterial10aAntigens, Bacterial10aArmadillos10aBacterial Proteins10aElectrophoresis, Polyacrylamide Gel10aEpitopes10aGlycoproteins10aHumans10aleprosy10aMycobacterium leprae10aXenarthra1 aChakrabarty A K1 aMaire M A1 aLambert P H00aSDS-PAGE analysis of M. leprae protein antigens reacting with antibodies from sera from lepromatous patients and infected armadillos.  a523-310 v493 a<p>Studies have been conducted to characterize M. leprae bacilli derived from infected armadillos. First, the proteins of the mycobacterial extracts were fractionated by SDS-PAGE. Subsequently, the proteins in the gel were electrophoretically transferred on a strip of nitrocellulose paper by the technique of 'electrophoretic blotting'. The separated bacterial protein bands, thus immobilized on the nitrocellulose paper were made to react immunologically with sera from the lepromatous patients, infected armadillo sera and other experimental mycobacterial antisera. It was observed that a majority of M. leprae proteins contained antigenic determinants also present on proteins of BCG. In addition, only two specific antigen bands of 33KD and 12KD were conspicuously detected by the patients' sera and the infected armadillo sera. These substances were further identified as polysaccharides or glycoproteins since they could only be stained by Schiff's reagent or alcian blue. Only 12KD glycoprotein band reacted with concanavalin A, whereas wheat germ agglutinin (WGA) did not show any reaction with them. These 33KD and 12KD glycoprotein antigens were found to lose their antigenicity after pepsin treatment and can be considered as glycoproteins. Further, radiolabelling experiments showed that 12KD antigen underwent radioiodination under usual conditions, but 33KD glycoprotein failed to be similarly radiolabelled. It is suggested that these protein antigens have M. leprae specific determinants on a cross-reacting component.</p>  a0009-9104