The investigation reveals different influence of the plague microbe's fraction 1 polysaccharide-protein complex and of it's purified protein on the 5'-nucleotidase activity and on the chemiluminescence response of peritoneal macrophages. Both of these metabolic indexes were found to be dependent on the dose of fraction 1 and duration of time till examination.
View Article and Find Full Text PDFThe association-dissociation processes involving the capsule antigen of Yersinia pestis were investigated. In aqueous salt solutions the material of the capsule (protein F1) exists in the form of associated species containing identical monomeric protein subunits. Brief heating (100 degrees C, 3 min) of F1 dissolved in buffered salt solutions at pHs between 4.
View Article and Find Full Text PDFMol Gen Mikrobiol Virusol
February 1987
Some properties of the structure of Y. pestis capsular antigen macromolecules have been studied. The aminoacid composition of F1 protein, the aminoacid sequence of the N-terminal fragment of antigen polipeptide chain were determined.
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