STRUCTURAL STUDIES OF RAT CATHEPSIN-E - AMINO-TERMINAL STRUCTURE AND CARBOHYDRATE UNITS OF MATURE ENZYME

被引：28

作者：

YONEZAWA, S

TAKAHASHI, T

ICHINOSE, M

MIKI, K

TANAKA, J

GASA, S

机构：

[1] UNIV TOKYO,FAC SCI,DEPT BIOPHYS & BIOCHEM,TOKYO 113,JAPAN

[2] UNIV TOKYO,FAC SCI,DEPT INTERNAL MED 1,TOKYO 113,JAPAN

[3] HOKKAIDO UNIV,SCH MED,INST CANC,SAPPORO,HOKKAIDO 060,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 166卷 / 02期

关键词：

D O I：

10.1016/0006-291X(90)90914-9

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：

The amino-terminal structure of rat gastric cathepsin E was identified and compared with the corresponding regions of human procathepsin E and other aspartic proteinases. The alignment revealed that cathepsin E has the most extended amino-terminal structure in aspartic proteinases, thus suggesting that the activation peptide (propeptide) of the human enzyme is 39-residues long. Analysis of oligosaccharide units suggested that rat cathepsin E possesses one N-linked carbohydrate unit, probably of the high mannose type. No evidence was obtained for the presence of O-linked sugars in rat cathepsin E. © 1990.

引用

页码：1032 / 1038

页数：7

共 15 条

[1]

AZUMA T, 1989, J BIOL CHEM, V264, P16748

[2] CLONING AND SEQUENCE-ANALYSIS OF CDNA FOR HUMAN CATHEPSIN-D [J].