Eighty-one bacterial strains representing 16 anaerobic species were tested in a sensitive binding assay for uptake of I-labelled human serum proteins. Fifteen of 36 strains (42%) bound significant amounts of human serum albumin (HSA). None of the other bacterial species showed any affinity for HSA. All strains studied were incapable of uptake of human fibrinogen, fibronectin, haptoglobin or aggregated β-microglobulin. strain Ra 4 was tested for binding of purified serum albumin from 11 animal species, and showed a binding profile similar to human group-C and -G streptococci, but different from and . Kinetic experiments showed that albumin binding was a rapid displaceable, time-dependent process, that could take place over a wide range of H or salt concentrations. The albumin-binding component of strain Ra 4 was resistant to heat and to periodate treatment, but sensitive to proteolytic enzymes.


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