The amino acid>s that constitute sequence gamma 268-282 of fibrinogen are not involved in fibrin monomer polymerization

• Autorzy: Janiak A. , Plucinski T. , Kupryszewski G. , Cierniewski C.S.
• Języki publikacji: EN

Abstrakty

EN

Congenitally abnormal fibrinogens with impaired fibrin monomer polymerization have been described to contain single amino-acid substitutions localized in certain positions of the γ275-330peptide region. To evaluate the role of the amino-acid sequence in the vicinity of Arg 275 in fibrin monomer polymerization, the peptide fragment corresponding to γ268-282was synthesized and used to obtain peptide-specific antibodies. These antibodies, when purified immunochemically on the immobilized peptide, bound to the intact fibrinogen and fibrin monomers with the same binding affinity. However, they did not recognize the Y268-282epitopes on the denatured and reduced fibrinogen molecules. The lack of influence of antipeptide antibodies on fibrin monomer polymerization indicates that the γ268-282peptide is not directly involved in the structure of the polymerization site in the D domain of fibrinogen. It is suggested that substitution of Arg275either by His or Cys in abnormal fibrinogens results probably in conformational changes which disturb a proper orientation of the polymerization site and reduce its expression.

Słowa kluczowe

EN

peptide; fibrinogen; amino acid; fibrin monomer polymerization; antibody

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1993
• Tom: 40
• Numer: 4
• Opis fizyczny: p.515-520,fig.

Twórcy

autor

Janiak A.

• Medical University in Lodz, 90-131 Lodz, Lindleya 3, Poland

autor

Plucinski T.

autor

Kupryszewski G.

autor

Cierniewski C.S.

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