The purification of fructose 1,6 diphosphatase from ox liver and its activation by ethylenediaminetetra acetate

Nimmo, H.G. and Tipton, K.F. (1975) The purification of fructose 1,6 diphosphatase from ox liver and its activation by ethylenediaminetetra acetate. Biochemical Journal, 145(2), pp. 323-334. (doi:10.1042/bj1450323) (PMID:239683) (PMCID:PMC1165221)

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Abstract

1.A procedure for the purification of ox liver fructose 1,6-kiphosphatase is described. A number of criteria indicate that the enzyme was not subjected to any significant degree of proteolytic attack during the purification. 2. The molecular weight, amino acid composition and subunit molecular weight are reported. 3. The activation by EDTA was shown to be due to the chelation heavy metals rather than by a more complex interaction with the enzyme as had previously been suggested.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Nimmo, Professor Hugh
Authors: Nimmo, H.G., and Tipton, K.F.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Biochemical Journal
Publisher:Portland Press
ISSN:0264-6021
ISSN (Online):1470-8728

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