SUMMARY: All 24 cultures of examined bound 1-labelled human albumin, IgG and fibrinogen; but neither IgA nor haptoglobin. Binding of human albumin was time-dependent, saturable and reversible by the addition of unlabelled albumin. The binding of 1-labelled human albumin could be inhibited completely by unlabelled albumin preparations from humans, mice and dogs, and partly by bovine albumin. In contrast, binding of 1-labelled human albumin was not inhibited by unlabelled rabbit albumin, human IgG or human fibrinogen. Data from competition experiments of two cultures with high 1-labelled albumin-binding activities yielded K values of 10 and 15 nmol l, respectively. The estimated number of binding sites per bacterial cell ranged from 30000 to 57000. The binding factor for albumin could be isolated from by boiling the bacteria at pH 2, and it was purified by affinity chromatography on human albumin-Sepharose. The isolated albumin-binding proteins had a molecular mass of approximately 5 1 kDa and inhibited binding of 1-labelled albumin to . They formed complexes with human albumin that altered its electrophoretic mobility.


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