Structure-Activity Relationships and Immunochemical Studies on Cobrotoxin
Abstract
Cobrotoxin, a neurotoxic crystalline protein, was isolated from the venom of Taiwan cobra (Naja naja atra) and was proved to be the main toxic protein in cobra venom. The two-dimensional structure of the toxin has recently been established, permits a study of structure-function relationships. Preceding studies on the chemical modification of the single tryptophan, tyrosyl and histidyl residues, free amino and carboxyl groups in cobrotoxin suggested that either the intact Trp-29, Tyr-25, His-32, epsilon-amino group of Lys-47 or gamma-carboxyl group of Glu-21 is essential for full activity of the toxin. Cobrotoxin is a basic protein having six arginine residues at the positions 28, 30, 33, 36, 39 and 59 in the sequence. In this study, selective and stepwise chemical modification of arginine residues were conducted with a group specific reagent, phenylglyoxal, at varying pH and the degree of modification in relation to the lethal activity and antigenic specificity has been studied in details.
Document Details
- Document Type
- Technical Report
- Publication Date
- Mar 05, 1974
- Accession Number
- AD0779433
Entities
People
- Chen-chung Yang
Organizations
- Kaohsiung Medical University