A cathepsin B-like proteinase was purified from eggs of Antheraea pernyi by 5 steps of purification. The molecular mass of the proteinase are estimated to be 47 kDa by using SDS-polyacrylamide gel electro-phoresis. Th...A cathepsin B-like proteinase was purified from eggs of Antheraea pernyi by 5 steps of purification. The molecular mass of the proteinase are estimated to be 47 kDa by using SDS-polyacrylamide gel electro-phoresis. The activity of the purified proteinase were strongly inhibited by E-64 and Leupeptin. The optimum pH is 3.5 as determined by using the bovine hemo-globin as substrate. The activity and quantity of the proteinase during embryo development were studied. The results suggested that the proteolytic activities during embryo development at least partially came from this proteinase.展开更多
文摘A cathepsin B-like proteinase was purified from eggs of Antheraea pernyi by 5 steps of purification. The molecular mass of the proteinase are estimated to be 47 kDa by using SDS-polyacrylamide gel electro-phoresis. The activity of the purified proteinase were strongly inhibited by E-64 and Leupeptin. The optimum pH is 3.5 as determined by using the bovine hemo-globin as substrate. The activity and quantity of the proteinase during embryo development were studied. The results suggested that the proteolytic activities during embryo development at least partially came from this proteinase.
