Galactose-6-phosphate dehydrogenase. Purification and partial characterization

Ray, M. ; Bhaduri, A. (1975) Galactose-6-phosphate dehydrogenase. Purification and partial characterization Journal of Biological Chemistry, 250 (10). pp. 3595-3601. ISSN 0021-9258

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Official URL: http://www.jbc.org/content/250/10/3595.abstract

Abstract

A new enzyme, galactose-6-phosphate dehydrogenase has been purified about 50-fold from goat liver. The enzyme can be distinguished from the nonspecific hexose-6-phosphate dehydrogenase and glucose-6-phosphate dehydrogenase by its high substrate specificity and absolute pyridine nucleotide requirement. In contrast to the hexose-6-phosphate dehydrogenase, this enzyme is located exclusively in the cytoplasmic fraction of the cell. The enzyme is a metalloprotein and is highly sensitive to mercurials. The product of the reaction is possibly a ketoaldose, phosphorylated at the primary alcoholic group.

Item Type:Article
Source:Copyright of this article belongs to American Society for Biochemistry and Molecular Biology.
ID Code:26456
Deposited On:06 Dec 2010 12:30
Last Modified:17 May 2016 09:45

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