Inactivation studies of cathepsin D with diazo compounds.
Cathepsin D was inactivated with various diazo compounds at very high concentration. Reaction proceeded maximally at pH 4.5 in the presence of cupric ions. With 3-diazo-indazole and triazene the inactivation was noted also in the absence of cupric ions what indicates that the mechanism is mediated through triazene. CD-spectrum of partially inactivated enzyme shows that conformational changes occurred after treatment with diazo compound.
D000818:Animals; D001391:Azo Compounds / Q000494:pharmacology*; D002403:Cathepsins / Q000037:antagonists & inhibitors*; D002417:Cattle; D002942:Circular Dichroism; D007700:Kinetics; D011487:Protein Conformation; D013154:Spleen / Q000201:enzymology; D013329:Structure-Activity Relationship; D014226:Triazenes / Q000494:pharmacology
D001391:Azo Compounds; D014226:Triazenes; D002403:Cathepsins