Characterization of monoclonal antibodies against β‐bungarotoxin and their use as structural probes for related phospholipase A2 enzymes and presynaptic phospholipase neurotoxins
- 1 July 1984
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 142 (1), 145-151
- https://doi.org/10.1111/j.1432-1033.1984.tb08262.x
Abstract
Mouse hybridoma lines secreting monoclonal antibodies against a phospholipase-inactive derivative of the presynaptic neurotoxin, .beta.-bungarotoxin, were established. These antibodies, of the IgG1 or IgG2b isotype with affinities in the range 1-2 .times. 108 l/mol, recognized a single immunodominant region of native .beta.-bungarotoxin, most probably located on the A (phospholipase homologue) chain of the toxin. Using plate-adsorbed radioimmunoassay procedures, antibodies reacted with native .beta.-bungarotoxin and other .beta.-bungarotoxin isotoxins and with the non-toxic phospholipase A also present in Bungarus multicinctus venom. Other phospholipase A enzymes and presynaptic phospholipase neurotoxins did not show any competition with .beta.-bungarotoxin in the radioimmunoassay. Globulin fractions of monoclonal antibodies partially inhibited the phospholipase activity of .beta.-bungarotoxin.Keywords
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