La cathepsine D de rate de cheval: II. - Étude de quelques propriétés enzymatiques
作者： André Ducastaing , Jean-Louis Azanza , Jacques Raymond , Jean-Michel Robin , Paul Créac'h
DOI: 10.1016/S0300-9084(76)80309-4
关键词: Catalysis 、 Stereochemistry 、 Active site 、 Polyphosphate 、 Substrate (chemistry) 、 Nitrite 、 Hydrolysis 、 Chemistry 、 Cathepsin 、 Enzyme
摘要: Summary This work reports some enzymatic properties of highly purified horse spleen cathepsin D. Hydrolysis rate several proteins are compared. The Kinetic constants (Km = 4.95 10 −5 M and Vm 1,76 ΔDO/mn/μg) have been determined in the presence a denatured haemoglobin substrate. Stability preparation is discussed according to pH, concentration time storage. Some investigations concerning active site described. Enzymatic chemical results show that dicarboxylic tryptophanyl residues seem be involved hydrolytic process. Catalysis does not depend on sulfhydryl or seryl residues. Different salts, particulary nitrate, nitrite polyphosphate potent inhibitors activity.
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