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Structural evidence for two isozymic forms and the carbohydrate attachment site of human gastric cathepsin E.

Abstract：

:The amino acid sequences in the NH2-terminal region and some other parts of human gastric cathepsin E were investigated. The NH2-terminal sequencing revealed that the cathepsin E preparation which had been activated at pH 4.0 contained one major and one minor isozymes in an approximate molar ratio of 3:1. The NH2-terminal sequence of the former was very similar to but partly different from that predicted from cDNA sequencing by Azuma et al., whereas the latter had an NH2-terminal sequence identical with the predicted sequence. These results provide structural evidence for the presence of at least two isozymic forms in human gastric cathepsin E. In addition, the site of carbohydrate attachment was elucidated by isolation and analysis of a glycopeptide fraction from an enzymatic digest of cathepsin E. A single carbohydrate chain was deduced to be attached to the asparagine residue at position 34 in the major isozyme and to the corresponding asparagine residue in the minor isozyme.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Athauda SB,Matsuzaki O,Kageyama T,Takahashi K

doi

10.1016/0006-291x(90)92403-m

subject

Has Abstract

pub_date

1990-04-30 00:00:00

pages

878-85

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(90)92403-M

journal_volume

168

pub_type

杂志文章

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