Common Antigenic Sites in Human, Bovine and Porcine Fibrinogens

Summary

Specific antisera to the Aα, Bβ and γ chains of porcine fibrinogen were used to characterize an antigenic homology of human, bovine, and porcine fibrinogens. Antigenic determinants shared by these fibrinogens were mostly formed by the Aα chain. However, in the case of bovine and porcine fibrinogens they were also found in the Bβ and γ polypeptide chains. The results reported here show that the Aα chain determinants exposed on the intact fibrinogen molecule are conserved to a considerably larger extent than those of the Bβ and γ chains.

Keywords

Mammalian fibrinogen - Polypeptide chains - Radioimmunoassay

• References

• 1 Doolittle RF, Fibrin ogen, and Fib rin. In: The Plasma Proteins, (Putnam FW). Vol. 02. pp 110-161 1975. Academic Press; New York:
• 2 Henschen A, Lottspeich F. Sequence homology between γ-chain and β-chain in human fibrin. Thromb Res 1977; 11: 869-880
• 3 Watt KWK, Takagi T, Doolittle RF. Amino acid sequence of the β chain of human fibrinogen: Homology with the y chain. Proc Natl Acad Sci USA 1978; 75: 1731-1735
• 4 Doolittle RF, Watt KWK, Cottrell BA, Strong DD, Riley M. The amino acid sequence of the γ-chain of human fibrinogen Nature. 1979; 280: 464-468
• 5 Gollwitzer R, Hahn E, Nowak H, Timpl R. Immunochemistry of bovine fibrinogen - 1. Immunogenic activity and diversity of antigenic determinants of reduced and carboxymethylated α, β and γ chains. Immunochemistry 1975; 12: 893-897
• 6 Atassi MZ. Antigenic structure of myoglob. In: The complete immunochemical anatomy of a protein and conclusions relating to antigenic structures of proteins. Immunochemistry. 1975. 12. 423-438
• 7 Gollwitzer R, Timple R, Becker U, Furthmayr H. Chemical and immunological properties of reduced and alkylated polypeptide chains of bovine fibrinogen. Eur J Biochem 1972; 28: 497-506
• 8 Gollwitzer R, Timpl R. Isolation and immunological characterization of a disulfide loop region in human fibrinogen α chain. FEBS lett 1975; 58: 269-272
• 9 Lotter H, Timpl R. Antigenic structure of the cyanogen bromide peptide F-CB3 from fibrinogen α-chain. Eur J Biochem 1975; 60: 221-226
• 10 Atassi Z. Precise determination of the entire antigenic structure of lisozyme. Immunochemistry 1978; 15: 909-936
• 11 Cierniewski CS, Edgington TS. Internalization of the amino terminal 1-78 sequence of the γ chain of native fibrinogen and exposure associated with catabolism and plasmin cleavage. Biochim Biophys Acta 1979; 580: 32-43
• 12 Henschen A. S-sulfo derivatives of fibrinogen and fibrin. Preparation and general properties. Ark Kemi 1964; 22: 1-28
• 13 Okude M, Jwanaga S. Carboxyl-terminal residues of mammalian fibrinogen and fibrin. Biochim Biophys Acta 1971; 251: 185-196
• 14 Cierniewski CS, Plow EP, Edgington TS. An immunochemical humology between the Aα and D:E complex-dependent site of the γ chains of fibrinogen. J Biol Chem 1977; 252: 8917-8923
• 15 Cierniewski CS, Krajewski T. Interaction of fibrinogen with fluorescein isothiocynate. Thromb Res 1978; 13: 615-624
• 16 Itzhaki RF, Gill DM. A microbiuret method for estimating proteins. Anal Biochem 1964; 9: 401-410
• 17 McDonagh J, Messel H, McDonagh R, Murano G, Blombäck B. Molecular weight analysis of fibrinogen and fibrin chains by an improved sodium dodecyl sulfate gel electrophoresis.. Biochim Biophys Acta 1972; 257: 135-142
• 18 Brummel MC, Montgomery R. Acrylamide gel electrophoresis of the S-sulfo derivatives of fibrinogen. Anal Biochem 1970; 33: 28-35
• 19 Plow EF, Edgington TS. Emergence of neoantigenic expressions during physiologic cleavages in vitro and in vivo. J Clin Invest 1973; 52: 273-282
• 20 Plow EF, Hougie C, Edgington TS. Neoantigenic expressions engendered by plasmin cleavage of fibrinogen. J Immunol 1971; 107: 1496-1500
• 21 Minden P, Farr RS. In: Handbook of Experimental Immunology/Weir DM/ pp. 463-492 F A. Davis Co; Philadelphia, Pa:
• 22 McConahey PJ, Dixon FJ. A method for trace iodination of proteins for immunologic studies. Int Arch Allergy Appl Immunol 1966; 29: 185-189