Proteins pp 355-360 | Cite as

A Method for Direct Amino Acid Sequence Analysis of the NH2-Terminal Regions of Fibrinogen

  • Chung Y. Liu
  • Francis J. Morgan


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.


Succinic Anhydride Pyroglutamic Acid Direct Sequence Analysis Human Fibrinogen Prior Separation 
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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Chung Y. Liu
    • 1
  • Francis J. Morgan
    • 1
  1. 1.College of Physicians and SurgeonsColumbia UniversityNew YorkUSA

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