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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Mao SY,Maki AH,de Haas GHdoi
10.1016/0014-5793(87)81279-6subject
Has Abstractpub_date
1987-01-19 00:00:00pages
83-8issue
1eissn
0014-5793issn
1873-3468journal_volume
211pub_type
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