Structure-Function Relationship of Hydrophiliidae Postsynaptic Neurotoxins
Abstract
This annual report is comprised of three parts: The hydrophilicity index of Lapemis toxin from Lapemis hardwickii sea snake and the alpha-subunit of the acetylcholine receptor of Torpedo californica have been determined and plotted versus of the sequence position. Lapemis toxin is a competitive inhibitor of alpha-bungarotoxin (alpha-aBTX) in binding to ACR. Two artinine residues out of three which are present in Lapemis toxin were modified by phenylglyoxal. The major neurotoxin was isolated from the sea snake venom of Acalyptophis peronii captured in the Gulf of Thailand. Partial N-terminal sequence of the toxin was identified up to 37 residues. Ten more residues beyond residue No. 37 were also identified, but the exact positions of these ten residues have not yet been identified.
Document Details
- Document Type
- Technical Report
- Publication Date
- Mar 05, 1987
- Accession Number
- ADA185198
Entities
People
- Anthony T. Tu
- Nobuhiro Mori
- Roger A. Miller
Organizations
- Colorado State University