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Characterization of the amino acids of bovine fibrinogen involved in the fibrinogen-thrombin interaction of the blood clotting process. Comparison with the milk clotting process

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Summary

Bovine fibrinogen and the Aα and Bβ chains of bovine fibrinogen have been subjected to chemical modification by a number of reagents and the effects of these procedures on the susceptibility of the proteins to thrombin hydrolysis is described. The reagents used were rose bengal (for photo-oxidation), 2-hydroxy-5-nitrobenzyl bromide, N-acetylimidazole, iodoacetic acid and diethyl pyrocarbonate. Evidence is presented which indicates that the tryptophan and tyrosine residues of fibrinogen are not involved to any great extent in the interaction of this protein with thrombin. Modification with iodoacetic acid suggests that methionine residues play a major role in such interactions, but the fibrinogen chains on which the important residues reside remain uncertain. The use of diethyl pyrocarbonate indicates the participation also of histidine in fibrinogen-thrombin interactions and that, whereas the histidine residues of the Bβ chain are involved to a great extent, it appears that those of the Aa chain are not. The similarities which exist between the fibrinogen-thrombin and the κ-casein-chymosin systems are discussed.

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Abbreviations

DEP:

diethyl pyrocarbonate (ethoxyformic anhydride)

HNBB:

2-hydroxy-5-nitrobenzyl bromide

N-Acl:

N-acetylimidazole

PTC:

phenylthiocarbamyl

PTH:

3-phenyl-2-thiohydantoin.

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Author notes

  1. Nicholas M. C. Kaye

    Present address: Department of Biochemistry, University of Leicester, LE1 7RH, Leicester, U.K.

Authors and Affiliations

  1. Laboratoire des Protéines, Université de Paris V, 45 rue des Saints-Pères, F-75270, Paris Cedex 06, France

    Nicholas M. C. Kaye & Pierre Jollès

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  1. Nicholas M. C. Kaye
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  2. Pierre Jollès
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Kaye, N.M.C., Jollès, P. Characterization of the amino acids of bovine fibrinogen involved in the fibrinogen-thrombin interaction of the blood clotting process. Comparison with the milk clotting process. Mol Cell Biochem 20, 173–182 (1978). https://doi.org/10.1007/BF00243764

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  • DOI: https://doi.org/10.1007/BF00243764

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