Marshall, D L and Harvey, A L (1992) Protease inhibitor homologues of dendrotoxin do not bind to dendrotoxin acceptors on synaptosomal membranes or facilitate neuromuscular transmission. Biological chemistry Hoppe-Seyler, 373 (8). pp. 707-714. ISSN 0177-3593Full text not available in this repository. (Request a copy from the Strathclyde author)
The dendrotoxins are a homologous group of potassium channel-blocking polypeptides found in mamba snake venom. They are similar in sequence and structure to Kunitz-type serine protease inhibitors. Modified and native protease inhibitors were assayed for dendrotoxin-like activity using radioligand-binding and twitch tension-recording methods. Despite the large number and high concentration of compounds tested, no protease inhibitor displayed dendrotoxin-like activity. The results indicate that the protease-inhibiting and potassium channel-blocking activities of these two groups of polypeptides are not linked.
|Keywords:||amino acid sequence, animals, chickens, elapid venoms, iodine radioisotopes, kinetics, membranes, molecular sequence data, muscle contraction, neuromuscular junction, potassium channels, protease inhibitors, radioligand assay, rats, cholinergic receptors, structure-activity relationship, synaptic transmission, synaptosomes, Biochemistry|
|Department:||Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences|
|Depositing user:||Pure Administrator|
|Date Deposited:||13 Jul 2011 08:56|
|Last modified:||27 Apr 2016 16:55|