Publication Date:
1982-08-20
Description:
Toxin isolated from cobra venom and labeled with tritium was incubated with membranes rich in acetylcholine receptors. The amount of toxin bound to the receptors was determined and the kinetics of dissociation of the receptor-toxin complex was followed. Addition of an excess of horse antiserum to the venom resulted in a significant acceleration of the dissociation reaction. Similarly, a monoclonal antibody against the toxin accelerated dissociation of the receptor-toxin complex. The results indicate that specific antibody binding destabilizes the toxin-receptor complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boulain, J C -- Menez, A -- New York, N.Y. -- Science. 1982 Aug 20;217(4561):732-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7100919" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Antibodies, Monoclonal/physiology
;
Cobra Neurotoxin Proteins/immunology/*metabolism
;
Cobra Venoms/immunology/*metabolism
;
Immunoglobulin Fab Fragments/physiology
;
Immunoglobulins/*physiology
;
In Vitro Techniques
;
Mice
;
Radioligand Assay
;
Receptors, Cholinergic/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
