Yeast phosphoglycerate kinase — evidence from affinity elution studies for conformational changes on binding of substrates

Scopes, Robert K.; Algar, Elizabeth

doi:10.1016/0014-5793(79)80736-x

Cited by 16 publications

(1 citation statement)

References 12 publications

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“…Using ion-exchange chromatography, Scopes & Algar (1979) found that the pH-dependent binding of PGK to the ion-exchange resin was substantially shifted when PGK was liganded with 1,3-P2G. Binding 3-PG, ATP, or ADP to PGK caused only a small shift in the affinity of PGK for the ionexchange resin.…”

Section: Discussionmentioning

confidence: 99%

Transfer of 1,3-diphosphoglycerate between glyceraldehyde 3-phosphate dehydrogenase and 3-phosphoglycerate kinase via an enzyme-substrate-enzyme complex

Weber¹,

Bernhard²

1982

Biochemistry

109

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On the basis of the alternatives of direct inter-enzyme transfer vs. dissociation followed by random diffusion, two kinetic models for metabolite transfer between consecutive enzymes are developed. These two models are readily distinguishable experimentally for the transfer of 1,3-diphosphoglycerate (1,3-P2G) between glyceraldehyde-3-phosphate dehydrogenase (GPDH) and 3-phosphoglycerate kinase (PGK). Since 1,3-P2G is exceedingly tightly bound to PGK, the kinetics of its transfer to GPDH are predictably different for each of these two models. Our experiments unambiguously demonstrate that 1,3-P2G is directly transferred between these two enzymes via an enzyme-substrate-enzyme complex. This direct transfer is described by a Michaelis-Menten scheme in which PGK . 1,3-P2G is the "substrate" for GPDH. At high concentrations of PGK . 1,3-P2G, the transfer reaction becomes nearly PGK . 1,3-P2G concentration independent. The rate of the transfer reaction is activated 3.5-fold by saturating quantities of ATP and 20-fold by saturating quantities of 3-PG. Evidence is presented that the PGK . 1,3-P2G complex is structurally distinct from either PGK itself or other PGK . ligand complexes.

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Section: Discussionmentioning

confidence: 99%

Transfer of 1,3-diphosphoglycerate between glyceraldehyde 3-phosphate dehydrogenase and 3-phosphoglycerate kinase via an enzyme-substrate-enzyme complex

Weber¹,

Bernhard²

1982

Biochemistry

109

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Chromatographic Purification of Virus Particles

Gagnon¹

2009

Encyclopedia of Industrial Biotechnology

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The application of chromatography represents an increasing trend in the field of virus purification. This article focuses on the unique constraints imposed by virus particles and how they relate to the strengths and limitations of various chromatography media. Specific attention is given to the contributions of different types of physical supports, including porous particles, monoliths, and adsorptive membranes. Media characteristics are also discussed in the context of purification process control, reproducibility, and process economics. Protocols are offered for conducting method development with size exclusion, ion exchange, hydrophobic interactions, hydroxyapatite, and bioaffinity chromatography, and guidelines are summarized for combining individual methods into integrated multistep purification procedures suitable for preparation of clinical material.

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Ion Exchange Chromatography

Karlsson

Hirsh²

2011

Methods of Biochemical Analysis

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Yeast phosphoglycerate kinase — evidence from affinity elution studies for conformational changes on binding of substrates

Cited by 16 publications

References 12 publications

Transfer of 1,3-diphosphoglycerate between glyceraldehyde 3-phosphate dehydrogenase and 3-phosphoglycerate kinase via an enzyme-substrate-enzyme complex

Transfer of 1,3-diphosphoglycerate between glyceraldehyde 3-phosphate dehydrogenase and 3-phosphoglycerate kinase via an enzyme-substrate-enzyme complex

Chromatographic Purification of Virus Particles

Ion Exchange Chromatography

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