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Interspecies Constancy of N-Terminal Amino-acid Sequences in the γ-Chain of Fibrinogen

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Abstract

THE fibrinogen molecule from several mammals is made up of three different peptide chains1,2, the α(A), β(B) and γ chains, which are cross-linked by disulphide bonds and possibly other bonds3–6. Previous comparative studies of the primary structure of fibrinogen have dealt with its N-terminal amino-acids2 and with amino-acid sequences of fibrinopeptides A and B, released from amino termini of the respective chains by the action of thrombin7. These have shown considerable interspecies variation in amino-acid sequences of the fibrinopeptides, except for a relatively constant C-terminal sequence in the fibrino-peptide A. We now report a second relatively constant sequence in the fibrinogen molecule, the amino terminus of its γ-chain.

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Author notes

  1. AGNES HENSCHEN

    Present address: St Vincent's School of Medical Research, Victoria Parade, Melbourne, 3065, Australia

Authors and Affiliations

  1. Department of Pathology, University of Louisville, Louisville, Kentucky

    HUBERT PIRKLE, AGNES HENSCHEN & AIJA POTAPOUS

Authors
  1. HUBERT PIRKLE
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  2. AGNES HENSCHEN
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  3. AIJA POTAPOUS
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PIRKLE, H., HENSCHEN, A. & POTAPOUS, A. Interspecies Constancy of N-Terminal Amino-acid Sequences in the γ-Chain of Fibrinogen. Nature 223, 400–401 (1969). https://doi.org/10.1038/223400a0

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