PMID:2831880
| Citation |
Nagao, Y, Nakada, T, Imoto, M, Shimamoto, T, Sakai, S, Tsuda, M and Tsuchiya, T (1988) Purification and analysis of the structure of alpha-galactosidase from Escherichia coli. Biochem. Biophys. Res. Commun. 151:236-41 |
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| 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. |
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| Keywords |
Amino Acid Sequence; Amino Acids/analysis; Chromatography, DEAE-Cellulose; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Escherichia coli/genetics; Galactosidases/isolation & purification; Genes, Bacterial; Molecular Weight; Plasmids; alpha-Galactosidase/analysis; alpha-Galactosidase/genetics; alpha-Galactosidase/isolation & purification |
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