Purification and analysis of the structure of alpha-galactosidase from Escherichia coli |
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| Authors: | Y Nagao T Nakada M Imoto T Shimamoto S Sakai M Tsuda T Tsuchiya |
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| Institution: | Department of Microbiology, Faculty of Pharmaceutical Sciences, Okayama University, Japan. |
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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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