Studies on bovine spleen cathepsin D.
The purification procedure of cathepsin D which includes autolysis results in the destruction of the molecule to smaller polypeptide chains. Pure catepsin D obtained by the method which includes affinity chromatography, contains single polypeptide chain of 42000 daltons. The N-terminal amino acid is glycine. The specificity was studied using synthetic substrates. CD measurement of cathepsin D shows mainly unordered structure, about 26% of beta-structure and only 5% of alpha-helix. Binding of pepstatin shows pronounced changes in the CD spectrum between 250 and 300 nm; above 7.5 no interaction was observed.
D000818:Animals; D002403:Cathepsins / Q000302:isolation & purification / Q000378:metabolism; D002417:Cattle; D002942:Circular Dichroism; D007700:Kinetics; D008970:Molecular Weight; D010436:Pepstatins; D011487:Protein Conformation; D013154:Spleen / Q000201:enzymology*; D013379:Substrate Specificity
D010436:Pepstatins; D002403:Cathepsins