Purification of cathepsin B by a new form of affinity chromatography.
Human cathepsin B was purified by affinity chromatography on the semicarbazone of Gly-Phe-glycinal linked to Sepharose 4B, with elution by 2,2'-dipyridyl disulphide at pH 4.0. The product obtained in high yield by the single step from crude starting material was 80-100% active cathepsin B. The possibility that this new form of affinity chromatography may be of general usefulness in the purification of cysteine proteinases is discussed.
D015082:2,2'-Dipyridyl / Q000031:analogs & derivatives; D002401:Cathepsin B; D002403:Cathepsins / Q000302:isolation & purification*; D002846:Chromatography, Affinity / Q000379:methods*; D004220:Disulfides; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D009842:Oligopeptides; D012664:Semicarbazones; D012685:Sepharose
D004220:Disulfides; D009842:Oligopeptides; D012664:Semicarbazones; C049913:glycyl-phenylalanyl-glycine-semicarbazone; C001105:2,2'-dipyridyl disulfide; D015082:2,2'-Dipyridyl; D012685:Sepharose; D002403:Cathepsins; D002401:Cathepsin B