Literature DB >> 24458448

Conditions leading to precipitation of ribulose bisphosphate carboxylase-oxygenase differ from those leading to enzyme activation.

J T Bahr1, D P Bourque.   

Abstract

The relation between conditions leading to precipitation and/or activation of Ru-P2 carboxylase have been explored in order to test the hypothesis that conformational changes leading to precipitation might be identical to those which are presumed to lead to enzyme activation. From the results of kinetic and solubility studies, we conclude that this hypothesis is not valid, since changes in solubility of Ru-P2 carboxylase occur ten times as fast as changes in enzyme kinetics.

Year:  1983        PMID： 24458448     DOI： 10.1007/BF00052373

Source DB:  PubMed          Journal:  Photosynth Res        ISSN： 0166-8595            Impact factor:   3.573


  18 in total

1.  Inactivation of ribulosebisphosphate carboxylase/oxygenase from spinach with the affinity label N-bromoacetylethanolamine phosphate.

Authors:  J V Schloss; F C Hartman
Journal:  Biochem Biophys Res Commun       Date:  1977-07-11       Impact factor: 3.575

2.  The use of 1-anilino-8-naphthalene sulfonate as fluorescent probe for conformational studies on ribulose-1,5-bisphosphate carboxylase.

Authors:  G F Wildner
Journal:  Z Naturforsch C Biosci       Date:  1976 May-Jun

3.  Specific effect of ribulose-1,5-diphosphate on the solubility of tobacco Fraction I protein.

Authors:  S Y Kwok; N Kawashima; S G Wildman
Journal:  Biochim Biophys Acta       Date:  1971-05-11

4.  D-Ribulose-1,5-bisphosphate carboxylase-oxygenase. Improved methods for the activation and assay of catalytic activities.

Authors:  G H Lorimer; M R Badger; T J Andrews
Journal:  Anal Biochem       Date:  1977-03       Impact factor: 3.365

5.  The role of effector molecules in regulating ribulosebisphosphate carboxylase activity.

Authors:  F Dailey; R S Criddle
Journal:  Arch Biochem Biophys       Date:  1980-05       Impact factor: 4.013

6.  Inhibition of ribulose-1,5-biphosphate carboxylase/oxygenase by ribulose-1,5-bisphosphate epimerization and degradation products.

Authors:  C Paech; J Pierce; S D McCurry; N E Tolbert
Journal:  Biochem Biophys Res Commun       Date:  1978-08-14       Impact factor: 3.575

7.  Effects of Mg2+ and substrates on the conformation of ribulose-1,5-bisphosphate carboxylase.

Authors:  A E Grebanier; D Champagne; H Roy
Journal:  Biochemistry       Date:  1978-11-28       Impact factor: 3.162

8.  A model for the kinetics of activation and catalysis of ribulose 1,5-bisphosphate carboxylase.

Authors:  W A Laing; J T Christeller
Journal:  Biochem J       Date:  1976-12-01       Impact factor: 3.857

9.  Regulation of ribulose 1,5-diphosphate carboxylase by substrates and other metabolites: further evidence for several types of binding sites.

Authors:  D K Chu; J A Bassham
Journal:  Plant Physiol       Date:  1975-04       Impact factor: 8.340

10.  Bicarbonate stabilization of ribulose 1,5-diphosphate carboxylase.

Authors:  W A Laing; W L Ogren; R H Hageman
Journal:  Biochemistry       Date:  1975-05-20       Impact factor: 3.162
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