Purification of a 29-kDa hemocyte proteinase of Sarcophaga peregrina.
Previously, we suggested the participation of a hemocyte proteinase in the dissociation of fat body of Sarcophaga peregrina (flesh fly) at metamorphosis. We have now purified this proteinase to near homogeneity from pupal hemocytes. It is a cysteine proteinase with a molecular mass of 29 kDa and has a unique substrate specificity hydrolyzing both Suc-Leu-Leu-Val-Tyr-MCA and Z-Phe-Arg-MCA (Suc, succinyl; MCA, methylcoumaryl-7-amide; Z, carbobenzoxy), which are substrates for chymotrypsin and cathepsin B, respectively. Partial similarity was found between the amino-terminal sequence of this proteinase and that of cathepsin B, including Pro, Glu and Arg residues conserved in the papain superfamily of enzymes.
Kurata
S
S
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Saito
H
H
Natori
S
S
D000595:Amino Acid Sequence; D000818:Animals; D002401:Cathepsin B / Q000378:metabolism; D002850:Chromatography, Gel; D002918:Chymotrypsin / Q000378:metabolism; D015891:Cystatins / Q000494:pharmacology; D003546:Cysteine Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D004175:Diptera / Q000201:enzymology*; D006458:Hemolymph / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012689:Sequence Homology, Nucleic Acid; D013379:Substrate Specificity
D015891:Cystatins; D002918:Chymotrypsin; D003546:Cysteine Endopeptidases; D002401:Cathepsin B