carbobenzoxy-Phe-Met methyl ester containing the bond involved in milk clotting mechanism is not hydrolyzed unless it becomes part of a polypeptide with tails of carbobenzoxy-Phe-Met anchored on a polylysine chain
small thin needle-like seed crystals of the native enzyme grown by the hanging-drop vapour-diffusion method, unit-cell dimensions a : 41.82 A, 51.21 A, c : 174.24 A, in complex with inhibitor pepstatin A, orthorhombic space group P2(1)2(1)2(1), isomorphous to native RMP crystals, unit-cell dimensions are a : 41.52 A, b : 50.82 A, c : 172.71 A
The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy) propane and pepstatin
Baudys, M.; Foundling, S.; Pavlik, M.; Blundell, T.; Kostka, V.
Protein chemical characterization of Mucor pusillus aspartic proteinase. Amino acid sequence homology with the other aspartic proteinases, disulfide bond arrangement and site of carbohydrate attachment