A Method for Direct Amino Acid Sequence Analysis of the NH2-Terminal Regions of Fibrinogen
Fibrinogen is one of the major plasma protein involved in blood coagulation and its primary structure has been completely determined 1–6 (Fig. 1). A number of abnormal fibrinogens have been purified and their structural defects have been found mainly in the NH2-terminal regions7, 8. However, fibrinogen is a macromolecule containing six polypeptide chains and the NH2-terminal amino acids of the two Bβ-chains are pyroglutamates which are not susceptible to direct sequence analysis by automated Edman degradation. In this report we present a simple method for the direct sequence analysis of the NH2 -terminal regions of fibrinogen without prior separation of the polypeptide chains to investigate the structural abnormalities of fibrinogen.
KeywordsHPLC EDTA Polypeptide Disulfide Anhydride
Unable to display preview. Download preview PDF.
- 1.F. Lottspeich, and A. Henschen, Amino Acid Sequence of Human Fibrin Preliminary Notes on the Completion of the γ-Chain Sequence, Hoppe-Seyler1s Z. Physiol. Chem. 358: 935 (1977).Google Scholar
- 7.C. Southan, A. Henschen, and F. Lottspeich, The Search for Molecular Defects in Abnormal Fibrinogens, in: “Fibrinogen”, A. Henschen, H. Graeff, and F. Lottspeich, eds., Walter de Gruyter, Berlin (1982).Google Scholar
- 8.C. Y. Liu, J.A. Koehn and H. L. Nossel, Abnormal Bβ-Chain in Fibrinogen New York (In Patients with a Thrombotic Tendency), Thromb. Haemost 50: 336 (1983).Google Scholar
- 17.C. Y. Liu, P. Wallen, and D.A. Handley, Fibrinogen New York 1: The Structural, Functional, and Genetic Defects and a Hypothesis of the Roles of Fibrin in Coagulation and Fibrinolysis, in: “Fibrinogen, Fibrin Formation and Fibrinolysis”, D. Lane, A. Henschen, and K. Jasani, eds., Walter de Gruyter, Berlin, In press (1985).Google Scholar