Purfication of synthetic cardiotoxin by affinity chromatography.
A polypeptide containing 60 amino acids with 4 disulphide bonds, synthesized by the solid-phase method, was highly purifed by anticardiotoxin-Sepharose affinity chromatography following gel filtration and CM-cellulose chromatography. The identification of the final product as cardiotoxin was confirmed by thin-layer chromatography on silica gel, polyacrylamide gel electrophoresis, amino acid analysis, circular dichroism spectra, N-terminal analysis and four biological tests.
D000818:Animals; D002645:Chickens; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004546:Elapid Venoms / Q000138:chemical synthesis / Q000302:isolation & purification / Q000494:pharmacology; D051379:Mice; D009119:Muscle Contraction / Q000187:drug effects; D013624:Taiwan
D004546:Elapid Venoms