Cathepsin E from rat neutrophils: Its properties and possible relations to cathepsin D-like and cathepsin E-like acid proteinases

Vitellogenin Transport and Yolk Formation in the Quail Ovary

“…Upon analysis by SDS-PAGE, both enzyme preparations were found to consist of three bands of 43, 30 and 14 kD. This seemed to be consistent with the known existence of single-chain (42 kD) and two-chain (30 and 12 kD) forms of mammalian cathepsin D (Yonezawa et al , 1987). However, the present study showed that the cathepsin D from quail liver and yolk consists only of a single-chain form of 40 kD.…”

“…Isolated yolks or the liver homogenates were mixed with two volumes of acetone, chilled to -20 ° C, and the supernatant was removed following centrifugation at 10,000xg for 10 min. Further purification of cathepsin D was performed with affinity chromatography on QA52 (Whatman, England) and pepstatin-Sepharose columns according to the method for the purification of Xenopus (Nakamura et al ., 1996) or rat (Yonezawa et al ., 1987) cathepsin D.…”

“…Monospecific anti-rat cathepsin D antibody was purified by using porcine liver cathepsin D-Sepharose 4B as an immunoadsorbent, as described previously (Yonezawa et al, 1987).…”

Foreign Peptides Expressed in Engineered Chimeric Self Molecules

“….Leu tetrapeplide. It is known that cathepsin D represents the major proteolytic lysosomal enzyme responsible for the antigen processing of foreign proteins (Yonezawa et at., 1987). No significant difference in the capacity of activating LDI-24 TcH was observed between the two constructs.…”

Proteolytic activity and cleavage specificity of cathepsin E at the physiological pH as examined towards the B chain of oxidized insulin

“…The optimum pH ofcathepsin E towards hemoglobin is 3-3.5, so its proteolytic activity and substrate speci- ficity were investigated previously only at acidic pHs [3,[12][13][14]. As far as cathepsin E can be active only at acidic pHs, its physiological roles in vivo would be highly restricted.…”