Reactivity of chemically cross-linked fibrinogen and its fragments D toward the staphylococcal clumping receptor.
It has been established that the binding domain for the staphylococcal clumping receptor exists in fragment D of human fibrinogen [Hawiger J., Timmons, S., Strong, D. D., Cottrell, B. A., Riley, M., & Doolittle, R. F. (1982) Biochemistry 21, 1407; Strong, D. D., Laudano, A., Hawiger, J., & Doolittle, R. F. (1982) Biochemistry 21, 1414]. To examine the role of valency in the adhesive function of fibrinogen, its fragments were prepared by digestion with plasmin in the presence of calcium and purified by a two-step chromatographic procedure. Fragments D1 and E did not induce the staphylococcal clumping reaction. After they were prepared in oligomeric form by chemical cross-linking with glutaraldehyde, fragment D1 (Mr 94,000) became functionally reactive toward the staphylococcal clumping receptor, and fragment D3 (Mr 75,000) and fragment E (Mr 50,000) remained inactive. Fragment D dimer derived from enzymatic cross-linking was not reactive. Human fibrinogen cross-linked with glutaraldehyde usually reached a 250 times higher reactivity toward the staphylococcal clumping receptor, depending on the condition of the cross-linking reaction. It is concluded that the valency of fibrinogen in regard to its receptor binding domain and the availability of this domain are essential for the staphylococcal clumping reaction.
D000447:Aldehydes / Q000494:pharmacology*; D003030:Coagulase / Q000378:metabolism*; D003432:Cross-Linking Reagents; D005338:Fibrin Fibrinogen Degradation Products / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism*; D005341:Fibrinolysin / Q000378:metabolism; D005976:Glutaral / Q000494:pharmacology*; D006801:Humans; D008970:Molecular Weight; D013211:Staphylococcus aureus
D000447:Aldehydes; D003030:Coagulase; D003432:Cross-Linking Reagents; D005338:Fibrin Fibrinogen Degradation Products; C046678:fibrinopeptide D; D005340:Fibrinogen; D005341:Fibrinolysin; D005976:Glutaral