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  • Title: Comparative optically detected magnetic resonance studies of mammalian phospholipase A2-lipid interactions.
    Author: Mao SY, Maki AH, de Haas GH.
    Journal: FEBS Lett; 1987 Jan 19; 211(1):83-8. PubMed ID: 3803590.
    Abstract:
    A major difference between porcine and bovine pancreatic phospholipase A2 (PA2) is the relatively low affinity of the bovine enzyme for lipid-water interfaces. We have investigated the binding of porcine, bovine, and equine PA2 to n-hexadecylphosphocholine (C16-PC) micelles using optically detected magnetic resonance (ODMR) spectroscopy. The zero field splittings (ZFS) of the single Trp-3 residue undergo significant changes upon binding of PA2 to C16-PC micelles. ZFS titrations of PA2 vs C16-PC indicate that porcine and equine enzymes have similar binding affinity and stoichiometry, while bovine PA2 binds much more weakly to the lipid-water interfaces. This may be attributed to the differences in the amino acid composition and the conformation of the binding sites for lipid-water interfaces of these enzymes.
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