The proteolytic action of Arvin on human fibrinogen |
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| Authors: | M R Ewart M W C Hatton J M Basford and K S Dodgson |
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| Institution: | Department of Biochemistry, University College, Cardiff CF1 1XL, U.K., and Twyford Laboratories Ltd., Twyford Abbey Road, London, N.W. 10, U.K. |
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| Abstract: | 1. Human fibrinogen was subjected to proteolysis by enzyme preparations (clinical Arvin and IRC-50 Arvin) from the venom of Agkistrodon rhodostoma. 2. IRC-50 Arvin releases three peptides from fibrinogen, and these were identified as fibrinopeptides AP, AY and A. 3. The less purified ;clinical' Arvin releases, in addition to fibrinopeptides AP, AY and A, small amounts of two heptapeptides derived from fibrinopeptides AP and A, probably because it contains another enzyme as well as Arvin. 4. No fibrinopeptide B is released by either Arvin preparation. 5. Thus, although Arvin is known to differ from ;reptilase' from Bothrops jararaca in that it does not activate the enzyme that cross-links fibrin (fibrin-stabilizing factor), it is identical with reptilase with respect to the peptides that it liberates from fibrinogen. |
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