Antigenic Structure of the Cyanogen Bromide Peptide F‐CB3 from Fibrinogen ‐Chain

Abstract

The antigenic properties of the cyanogen bromide peptide F‐CB3 from bovine fibrinogen a‐chain were studied in radioimmune assays with rabbit antibodies to fibrinogen or to peptide F‐CB3. Both fibrinogen and peptide F‐CB3 were indistinguishable in inhibition and dissociation tests. Modification of the single disulfide bridge in peptide F‐CB3 either by reduction or by cleavage with cyanide was not accompanied by loss of serologic activity. Inhibition studies with three individual fragments obtained after cyanide cleavage (molecular weight range 7000 to 23000) indicated the presence of at least three distinct antigenic determinants in peptide F‐CB3. After trypsin digestion of peptide F‐CB 3 still 75 % of its maximal inhibiting capacity was retained. Lack of change in antigenic activity of peptide F‐CB3 after release from the fibrinogen molecule by cyanogen bromide and upon further fragmentation is presumably due to the presence of several sequential antigenic determinants but the presence of conformational determinants could not be entirely excluded. Since no cross‐reaction was observed between bovine and human peptides F‐CB3 one may expect considerable variation in their amino acid sequence.