Abstract
Phospholipase A2 activation by membrane-bound peptides was investigated in order to understand the role of the membrane-induced conformation on activation, and to examine the occurrence of a peptide-enzyme complex at the lipid/water interface. For the peptides studies, bee venom phospholipase A2 was stimulated regardless of the membrane-bound conformation (alpha-helix, beta-sheet or random coil). Using antisera raised against melittin, we were able to demonstrate the occurrence of a calcium-dependent complex involving the enzyme, phospholipid substrate, and peptide.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Antibodies / immunology
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Bee Venoms / enzymology*
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Circular Dichroism
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Enzyme Activation
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Liposomes / metabolism
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Melitten / immunology
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Melitten / pharmacology*
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Membrane Proteins / metabolism
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Molecular Sequence Data
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Peptides / chemistry
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Peptides / metabolism
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Phospholipases A / antagonists & inhibitors
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Phospholipases A / chemistry
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Phospholipases A / metabolism*
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Phospholipases A2
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Protein Conformation
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Protein Structure, Secondary
Substances
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Antibodies
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Bee Venoms
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Liposomes
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Membrane Proteins
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Peptides
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Melitten
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Phospholipases A
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Phospholipases A2