title: [Isolation of cathepsin D from the aorta using pepstatin sepharose].
abstract: Affinity chromatography on pepstatin-Sepharose was used for isolation of cathepsin D from pig aorta. The enzyme was purified 800-fold. The proteolytic activity of cathepsin D was completely inhibited by pepstatin, suggesting that there were no other proteinases in the enzyme preparation obtained.
mesh_terms: D000818:Animals; D001011:Aorta / Q000201:enzymology*; D002403:Cathepsins / Q000302:isolation & purification*; D002846:Chromatography, Affinity / Q000379:methods; D004789:Enzyme Activation; D009842:Oligopeptides; D010436:Pepstatins; D011134:Polysaccharides; D012685:Sepharose; D013552:Swine
chemical_list: D009842:Oligopeptides; D010436:Pepstatins; D011134:Polysaccharides; D012685:Sepharose; D002403:Cathepsins
vernacular_title: Vydelenie katepsina D iz aorty s pomoshch'iu pepstatin-sefarozy.