Soltkz, L. V., Schalen, C. & MBrdh, P.-A. An effective, selective medium for Yersinia enterocolitica containing sodium oxalate. Acta path. microbiol. scand. Sect. B, 88: 11-16, 1980. A medium O)Y(c medium) is described, which was more efficient for the isolation of Yersinia enterocolitica from experimentally infected faecal specimens than desoxycholate-citrate, McConkey , lactose-sucrose-urea (LSU) agar, and Yersinia selective medium (Wauter's medium). The DY(C medium consists of casein hydrolysate and peptone serving as carbon and energy sources. A high selectivity is achieved by its contents of sodium oxalate and bile salts. The oxalate suppresses growth of gramnegative rods, including members of the family Ennterobacteriaceae and of Pseudomonas spp., while the bile salts inhibit growth of gram-positive bacteria. In the few instances coliform rods grew on the VYCC medium, they could easily be distinguished by their fermentation of lactose, included in the medium, and the fact that colonies of organisms were surrounded by an opaque zone of precipitated bile salts. The most optimal condition for the isolation of Y. enterocolitica from stools was achieved at incubation of the ~Ytc medium at 29 O C for 2 days.
Lysolecithin exhibits a lytic activity on acholeplasmas and mycoplasmas. The acholeplasmas studied, viz. Acholeplasma laidlawii A and B, were found less susceptible than were the mycoplasmas, viz. Mycoplasma gallisepticum and M. pneumoniae. The sensitivitxy to lysis was found to differ according to species, growth temperature and number of organisms used. Variations in age of the population and the concentration of bivalent ions in the test medium had but little influence. The greatest lytic activity of lysolecithin was found at the optimal growth temperature and decreased with lowering of the temperature. This lytic activity was inversely proportional to the density of the cell suspensions used. The possible mechanism of the lytic effect of lysolecithin is discussed.
The interaction between streptococci and human IgG, which does not involve the antibody combining sites, was visualized in the electron microscope by the use of human IgG myeloma proteins and ferritin labelled rabbit anti‐human IgG antibodies. The streptococci were allowed to react with human IgG myeloma proteins and the human IgG was then marked by addition of ferritin labelled rabbit anti‐human IgG antibodies; sections of streptococci studied in electron microscopy showed localization of the ferritin on the surface of the cell wall of all the streptococci of type M1, M 3, M 12 and M 56 studied. Similar results were obtained if the ferritin‐labelled rabbit anti‐human IgG antibodies alone were allowed to react with the streptococci. The uptake of ferritin labelled rabbit anti‐human IgG antibodies could be inhibited by addition of normal rabbit serum.
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