title: 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.affiliation: Department of Microbiology, Faculty of Pharmaceutical Sciences, Okayama University, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Nagao
authors.forename: T
authors.initials: T
authors.lastname: Nakada
authors.forename: M
authors.initials: M
authors.lastname: Imoto
authors.forename: T
authors.initials: T
authors.lastname: Shimamoto
authors.forename: S
authors.initials: S
authors.lastname: Sakai
authors.forename: M
authors.initials: M
authors.lastname: Tsuda
authors.forename: T
authors.initials: T
authors.lastname: Tsuchiya
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005696:Galactosidases / Q000302:isolation & purification*; D005798:Genes, Bacterial; D008970:Molecular Weight; D010957:Plasmids; D000519:alpha-Galactosidase / Q000032:analysis / Q000235:genetics / Q000302:isolation & purification*
chemical_list: D000596:Amino Acids; D005696:Galactosidases; D000519:alpha-Galactosidase