Purification and analysis of the structure of alpha-galactosidase from Escherichia coli.

Abstract:

:Alpha-Galactosidase, the product of the melA gene, was purified from a strain of Escherichia coli harboring a plasmid carrying melA, which over-produced the alpha-galactosidase. An apparent molecular weight was determined to be 50 kDa. The amino acid composition of this enzyme was determined. The result indicates that this enzyme is a hydrophilic and acidic protein. We have subjected the purified enzyme to 20 cycles of N-terminal sequence analysis. This verified the translation start site of the melA gene and the predicted N-terminal sequence.

authors

Nagao Y,Nakada T,Imoto M,Shimamoto T,Sakai S,Tsuda M,Tsuchiya T

doi

10.1016/0006-291x(88)90584-0

subject

Has Abstract

pub_date

1988-02-29 00:00:00

pages

236-41

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(88)90584-0

journal_volume

151

pub_type

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