Affordable Access

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

Authors
  • Nagao, Y
  • Nakada, T
  • Imoto, M
  • Shimamoto, T
  • Sakai, S
  • Tsuda, M
  • Tsuchiya, T
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Feb 29, 1988
Volume
151
Issue
1
Pages
236–241
Identifiers
PMID: 2831880
Source
Medline
License
Unknown

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.

Report this publication

Statistics

Seen <100 times