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  • Title: A further examination of the active form of Crotalus adamanteus phospholipase A2.
    Author: Smith CM, Wells MA.
    Journal: Biochim Biophys Acta; 1981 Mar 23; 663(3):687-94. PubMed ID: 7225406.
    Abstract:
    The phospholipase A2 from Crotalus adamanteus venom has been shown to be active as the dimer or 30 000 molecular weight species, at concentrations used for enzyme assay (0.1--10 microgram/ml). Gel filtration of the enzyme in the presence of Ca2+ and monomeric concentrations of the substrate dihexanoylphosphatidylcholine showed that all the protein migrated as a 30 000 molecular weight species. Active enzyme sedimentation velocity experiments using the same conditions gave s020,W=2.85 +/- 0.05 S, which compares favorably with the value obtained at mg/ml concentrations (3.11 S). These results confirm the results of Shen et al. (Shen, B.W., Tsao, F.H.C, Law, J.H. and Kézdy, F.J. (1975) J. Am. Chem. Soc. 97, 1205--1208).
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