Fig. 6.
Fig. 6. S sanguis binding to glycocalicin. / (A) Binding of fluorescently labeled strains of S sanguis (SK96 and NCTC 7863 do not adhere to platelets) to glycocalicin. The P value is for the comparison of 133-79 with SK96 and NCTC 7863. (B) Binding of biotin-S sanguis to glycocalicin (apparent molecular weight, 118 kd) Western blotted from 7.5% SDS-PAGE gel. The blot was probed with lane 1, anti-GPIb (P6/40); lane 2, biotinylated S sanguis 133-79 cells; lane 3, biotinylated S sanguis NCTC 7863 cells, and lane 4, PBS. After washing, lane 1 was probed with horseradish peroxidase–conjugated goat antimouse IgG and lanes 2 to 4 were probed with horseradish peroxidase–conjugated avidin. All lanes were then developed in chlor-1-naphthol and H2O2.

S sanguis binding to glycocalicin.

(A) Binding of fluorescently labeled strains of S sanguis (SK96 and NCTC 7863 do not adhere to platelets) to glycocalicin. The P value is for the comparison of 133-79 with SK96 and NCTC 7863. (B) Binding of biotin-S sanguis to glycocalicin (apparent molecular weight, 118 kd) Western blotted from 7.5% SDS-PAGE gel. The blot was probed with lane 1, anti-GPIb (P6/40); lane 2, biotinylated S sanguis 133-79 cells; lane 3, biotinylated S sanguis NCTC 7863 cells, and lane 4, PBS. After washing, lane 1 was probed with horseradish peroxidase–conjugated goat antimouse IgG and lanes 2 to 4 were probed with horseradish peroxidase–conjugated avidin. All lanes were then developed in chlor-1-naphthol and H2O2.

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