Inactivation of cathepsin B by oxidized LDL involves complex formation induced by binding of putative reactive sites exposed at low pH to thiols on the enzyme

Free Radical Biology and Medicine

Volumn 23, Issue 2, 1997, Pages 215-225

  O'Neil, June ^a   Hoppe, George ^a   Sayre, Lawrence M ^b   Hoff, Henry F ^a  

^a LERNER RESEARCH INSTITUTE   (United States)

^b CASE WESTERN RESERVE UNIVERSITY   (United States)

Author keywords

4 Hydroxynonenal; Cathepsin B; Enzyme inactivation; N Ethylmaleimide; Oxidized LDL; Reduction with NaBH4; Thiols

Indexed keywords

CATHEPSIN B; OXIDIZED LOW DENSITY LIPOPROTEIN;

ARTICLE; COMPLEX FORMATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME INACTIVATION; PH; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; PROTEIN MODIFICATION; RADIOIODINATION;

ALDEHYDES; ANIMALS; APOLIPOPROTEINS B; BINDING SITES; CATHEPSIN B; CATTLE; FREE RADICALS; HYDROGEN-ION CONCENTRATION; KINETICS; LIPOPROTEINS, LDL; MICE; MODELS, CHEMICAL; OXIDATION-REDUCTION; REACTIVE OXYGEN SPECIES; SERUM ALBUMIN, BOVINE; SULFHYDRYL COMPOUNDS;

EID: 0030976980     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(96)00612-0     Document Type: Article

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