Wheat germ phosphoglycerate mutase: Purification, polymorphism, and inhibition

Smith, George W.; Hass, Louis F.

doi:10.1016/0006-291x(85)91301-4

Cited by 11 publications

(13 citation statements)

References 10 publications

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“…In both cases the final specific activity, assayed at pH 8.7 (Smith & Hass, 1985), was approx. 3000 units/mg.…”

Section: Methodsmentioning

confidence: 90%

“…Assays of 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity were initially performed under the conditions described by Smith & Hass (1985), i.e. with 20 mM-3-phosphoglycerate, 8.3 mM-MgSO4 and 40,g of enolase in 0.1 M-Tris/HCl buffer, pH 8.7 (total volume 1.0 ml).…”

Section: Methodsmentioning

confidence: 99%

“…Phosphoglycerate mutase from wheat germ Phosphoglycerate mutase was purified from wheat germ by the methods of Leadlay et a.. (1977) and of Smith & Hass (1985). In both cases the final specific activity, assayed at pH 8.7 (Smith & Hass, 1985), was approx.…”

Section: Methodsmentioning

confidence: 99%

“…The enzymes from two species of Bacillus are dependent on Mn2+ for activity (Singh & Setlow, 1979;Watabe & Freese, 1979). Smith & Hass (1985) showed that the enzyme from wheat germ lost activity on incubation with various chelating agents such as EDTA and HQSA. We have also shown that some other 2,3-bisphosphoglycerate-independent enzymes are inactivated by these chelating agents .…”

Section: Introductionmentioning

confidence: 99%

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Do metal ions promote the re-activation of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutases?

Johnson

Price

1988

Biochemical Journal

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It has been reported [Smith, McWilliams & Hass (1986) Biochem. Biophys. Res. Commun. 136, 336-340] that addition of certain metal ions, notably Co2+ and Mn2+, promoted the refolding of denatured phosphoglycerate mutase from wheat germ. We have re-investigated these experiments and have shown that, when precautions are taken to avoid artefacts in the assay system, the metal ions do not promote any re-activation of the denatured wheat-germ or Aspergillus nidulans enzymes. An alternative explanation is offered for the observations of Smith et al. (1986).

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“…In both cases the final specific activity, assayed at pH 8.7 (Smith & Hass, 1985), was approx. 3000 units/mg.…”

Section: Methodsmentioning

confidence: 90%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Do metal ions promote the re-activation of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutases?

Johnson

Price

1988

Biochemical Journal

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“…For metabolite assays, 2,3-biphosphoglycerate-independent phosphoglycerate mutase was purified from wheat germ as described by Ruuska (1998) using methods based on those of Grisolia and Carreras (1975), Leadlay et al (1977), Smith and Hass (1985), and Grana et al (1989), with an additional step to remove adenylate kinase by adsorption to a HiTrap Blue (Pharmacia Biotech, Piscataway, NJ) affinity column.…”

Section: Luminometric Determination Of 3-phosphoglycerateolate (Pga) mentioning

confidence: 99%

The Role of Chloroplast Electron Transport and Metabolites in Modulating Rubisco Activity in Tobacco. Insights from Transgenic Plants with Reduced Amounts of Cytochrome b/fComplex or Glyceraldehyde 3-Phosphate Dehydrogenase

et al. 2000

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Leaf metabolites, adenylates, and Rubisco activation were studied in two transgenic tobacco (Nicotiana tabacum L. cv W38) types. Plants with reduced amounts of cytochrome b/f complex (anti-b/f) have impaired electron transport and a low transthylakoid pH gradient that restrict ATP and NADPH synthesis. Plants with reduced glyceraldehyde 3-phosphate dehydrogenase (anti-GAPDH) have a decreased capacity to use ATP and NADPH in carbon assimilation. The activation of the chloroplast NADP-malate dehydrogenase decreased in anti-b/f plants, indicating a low NADPH/ NADP ؉ ratio. The whole-leaf ATP/ADP in anti-b/f plants was similar to wild type, while it increased in anti-GAPDH plants. In both plant types, the CO 2 assimilation rates decreased with decreasing ribulose 1,5-bisphosphate concentrations. In anti-b/f plants, CO 2 assimilation was further compromised by reduced carbamylation of Rubisco, whereas in anti-GAPDH plants the carbamylation remained high even at subsaturating ribulose 1,5-bisphosphate concentrations. We propose that the low carbamylation in anti-b/f plants is due to reduced activity of Rubisco activase. The results suggest that light modulation of activase is not directly mediated via the electron transport rate or stromal ATP/ADP, but some other manifestation of the balance between electron transport and the consumption of its products. Possibilities include the transthylakoid pH gradient and the reduction state of the acceptor side of photosystem I and/or the degree of reduction of the thioredoxin pathway.

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