Biochem Biophys Res Commun. 1988 Feb 29;151(1):236-41.

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

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

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Department of Microbiology, Faculty of Pharmaceutical Sciences, Okayama University, Japan.

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.

PMID:: 2831880; [PubMed - indexed for MEDLINE]

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