PURIFICATION OF A 29-KDA HEMOCYTE PROTEINASE OF SARCOPHAGA-PEREGRINA

被引：33

作者：

KURATA, S ^{[1
]}

SAITO, H ^{[1
]}

NATORI, S ^{[1
]}

机构：

[1] UNIV TOKYO,FAC PHARMACEUT SCI,BUNKYO KU,TOKYO 113,JAPAN

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 204卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1992.tb16711.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Previously, we suggested the participation of a hemocyte proteinase in a 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 catepsin B, including Pro, Glu and Arg residues conserved in the papain superfamily of enzymes.

引用

页码：911 / 914

页数：4

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