STRUCTURE-ACTIVITY RELATIONSHIPS AND IMMUNOCHEMICAL STUDIES ON COBROTOXIN
Abstract
The amino acid sequence of cobrotoxin has recently been established. However, in consideration that the disulfide bonds are the major bonds which maintain the protein in its native configuration and that the integrity of the disulfide bonds is important for the venom toxicity, it is essential that each pair of the half-cystinyl residues be determined to assist in the elucidation of the two-dimensional structure of cobrotoxin. Cobrotoxin was digested with acid protease A and the resulting five cystine peptides were separated by high- voltage paper electrophoresis. The identification of the disulfide bridges was made by determining the amino acid composition of the corresponding cysteic acid peptides obtained after the oxidation of the single cystine peptides. Five cystine peptides were obtained from which the two remaining disulfide bridges were established. The specificity of the acid protease A, the selectivity of acid hydrolysis, and the structure of cobrotoxin are discussed.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 01, 1970
- Accession Number
- AD0710330
Entities
People
- Chen-chung Yang
Organizations
- Kaohsiung Medical University