PMID: 2510158Oct 1, 1989Paper

Agkistrodon piscivorus piscivorus platelet aggregation inhibitor: a potent inhibitor of platelet activation

Proceedings of the National Academy of Sciences of the United States of America
B H ChaoJ M Maraganore

Abstract

Applaggin (Agkistrodon piscivorus piscivorus platelet aggregation inhibitor) is a potent inhibitor of platelet activation. The protein is isolated from the venom of the North American water moccasin snake in three steps, including gel filtration, cation exchange, and reverse-phase HPLC procedures. The purified protein migrates as a 17,700-Da polypeptide by SDS/PAGE under nonreducing conditions and as a 9800-Da peptide in the presence of thiol. The behavior of applaggin on SDS/PAGE would indicate that the protein is a disulfide-linked dimer. Applaggin has been completely sequenced by Edman degradation and consists of 71 amino acids. The sequence is rich in cysteine and contains Arg-Gly-Asp at residues 50-52. Applaggin blocks platelet aggregation induced by ADP, collagen, thrombin, or arachidonic acid with IC50 values ranging from 12 to 128 nM (0.2-2.3 micrograms/ml) depending on the agonist and its concentration. This inhibition is found to correlate with inhibition of thromboxane A2 generation and of dense granule release of serotonin. Inhibition by applaggin of serotonin release induced by ADP, gamma-thrombin, and collagen was monitored in plasma under stirred conditions with [3H]serotonin-loaded platelets, and IC50 values for...Continue Reading

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Citations

Jan 1, 1994·Journal of Clinical Pharmacology·L A Harker
Mar 1, 1994·Medicinal Research Reviews·D CoxK Yoshida
Jan 1, 1990·Toxicon : Official Journal of the International Society on Toxinology·R M Kini, H J Evans
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Apr 4, 2021·International Journal of Molecular Sciences·Danique L van den KerkhofIngrid Dijkgraaf

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