Literature DB >> 7044813

Reactivation of yeast glucose-6-phosphate dehydrogenase denaturated by saturated fatty acids.

P Tortora, N Burlini, G M Hanozet, A Guerritore.   

Abstract

Activity of yeast glucose-6-phosphate dehydrogenase, inactivated by treatment with saturated fatty acids, can be partially restored by incubation in a medium of suitable ionic composition. The effectiveness of ions in the reactivation process is inversely related to their 'chaotropic' properties. Time-dependence of reactivation extent suggests a 2-step mechanism of enzyme inactivation and the existence of an intermediate form that aggregates through a 2nd-order reaction, producing irreversibly inactive enzyme.

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Year:  1982        PMID: 7044813     DOI: 10.1007/bf01952620

Source DB:  PubMed          Journal:  Experientia        ISSN: 0014-4754


  5 in total

1.  Glucose 6-phosphate dehydrogenase from brewers' yeast (Zwischenferment). 3. Studies on the subunit structure and on the molecular association phenomenon induced by triphosphopyridine nucleotide.

Authors:  R H Yue; E A Noltmann; S A Kuby
Journal:  J Biol Chem       Date:  1969-03-10       Impact factor: 5.157

2.  Solubilization of particulate proteins and nonelectrolytes by chaotropic agents.

Authors:  Y Hatefi; W G Hanstein
Journal:  Proc Natl Acad Sci U S A       Date:  1969-04       Impact factor: 11.205

3.  Dissociation and association of fumarase subunits with special reference to the formation of a functional tetramer.

Authors:  S Yamato; T Murachi
Journal:  Eur J Biochem       Date:  1979-01-02

4.  Glucose 6-phosphate dehydrogenase (Zwischenferment). II. Homogeneity measurements and physical properties of the crystalline apoenzyme from yeast.

Authors:  R H Yue; E A Noltmann; S A Kuby
Journal:  Biochemistry       Date:  1967-04       Impact factor: 3.162

5.  Selective denaturation of several yeast enzymes by free fatty acids.

Authors:  P Tortora; G M Hanozet; A Guerritore; M T Vincenzini; P Vanni
Journal:  Biochim Biophys Acta       Date:  1978-08-07
  5 in total

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