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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

Abstract

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.

Keywords

Succinic Anhydride Pyroglutamic Acid Direct Sequence Analysis Human Fibrinogen Prior Separation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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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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