Literature DB >> 16667877

Polysaccharide Fraction from Higher Plants which Strongly Interacts with the Cytosolic Phosphorylase Isozyme : I. Isolation and Characterization.

Y Yang1, M Steup.   

Abstract

From leaves of Spinacia oleracea L. or from Pisum sativum L. and from cotyledons of germinating pea seeds a high molecular weight polysaccharide fraction was isolated. The apparent size of the fraction, as determined by gel filtration, was similar to that of dextran blue. Following acid hydrolysis the monomer content of the polysaccharide preparation was studied using high pressure liquid and thin layer chromatography. Glucose, galactose, arabinose, and ribose were the main monosaccharide compounds. The native polysaccharide preparation interacted strongly with the cytosolic isozyme of phosphorylase (EC 2.4.1.1). Interaction with the plastidic phosphorylase isozyme(s) was by far weaker. Interaction with the cytosolic isozyme was demonstrated by affinity electrophoresis, kinetic measurements, and by (14)C-labeling experiments in which the glucosyl transfer from [(14)C]glucose 1-phosphate to the polysaccharide preparation was monitored.

Entities:  

Year:  1990        PMID: 16667877      PMCID: PMC1077328          DOI: 10.1104/pp.94.3.960

Source DB:  PubMed          Journal:  Plant Physiol        ISSN: 0032-0889            Impact factor:   8.340


  13 in total

1.  Localization of alpha-Amylase in the Apoplast of Pea (Pisum sativum L.) Stems.

Authors:  E P Beers; S H Duke
Journal:  Plant Physiol       Date:  1988-08       Impact factor: 8.340

2.  Subcellular localization and characterization of amylases in Arabidopsis leaf.

Authors:  T P Lin; S R Spilatro; J Preiss
Journal:  Plant Physiol       Date:  1988-01       Impact factor: 8.340

3.  Subcellular localization of the starch degradative and biosynthetic enzymes of spinach leaves.

Authors:  T W Okita; E Greenberg; D N Kuhn; J Preiss
Journal:  Plant Physiol       Date:  1979-08       Impact factor: 8.340

4.  Neurospora crassa glucogen phosphorylase: interconversion and kinetic properties of the "active" form.

Authors:  M H Gold; R J Farrand; J P Livoni; I H Segel
Journal:  Arch Biochem Biophys       Date:  1974-04-02       Impact factor: 4.013

5.  Simple rapid method for the separation and quantitative analysis of carbohydrates in biological fluids.

Authors:  Z Zilić; N Blau; M Knob
Journal:  J Chromatogr       Date:  1979-09-11

6.  Modifications of the Park-Johnson ferricyanide submicromethod for the assay of reducing groups in carbohydrates.

Authors:  M Porro; S Viti; G Antoni; P Neri
Journal:  Anal Biochem       Date:  1981-12       Impact factor: 3.365

7.  Characterization of the spinach leaf phosphorylases.

Authors:  J Preiss; T W Okita; E Greenberg
Journal:  Plant Physiol       Date:  1980-11       Impact factor: 8.340

8.  Water stress enhances expression of an alpha-amylase gene in barley leaves.

Authors:  J V Jacobsen; A D Hanson; P C Chandler
Journal:  Plant Physiol       Date:  1986-02       Impact factor: 8.340

9.  Characterization of Pea Chloroplast D-Enzyme (4-alpha-d-Glucanotransferase).

Authors:  G Kakefuda; S H Duke
Journal:  Plant Physiol       Date:  1989-09       Impact factor: 8.340

10.  Enzymic determination of inorganic phosphates, organic phosphates and phosphate-liberating enzymes by use of nucleoside phosphorylase-xanthine oxidase (dehydrogenase)-coupled reactions.

Authors:  H de Groot; H de Groot; T Noll
Journal:  Biochem J       Date:  1985-08-15       Impact factor: 3.857

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  14 in total

1.  Glucan-phosphorylase forms in cotyledons of Pisum sativum L.: Localization, developmental change, in-vitro translation, and processing.

Authors:  J van Berkel; J Conrads-Strauch; M Steup
Journal:  Planta       Date:  1991-10       Impact factor: 4.116

2.  The starch phosphorylase gene is subjected to different modes of regulation in starch-containing tissues of potato.

Authors:  B St-Pierre; C Bertrand; A Camirand; M Cappadocia; N Brisson
Journal:  Plant Mol Biol       Date:  1996-03       Impact factor: 4.076

3.  A second L-type isozyme of potato glucan phosphorylase: cloning, antisense inhibition and expression analysis.

Authors:  U Sonnewald; A Basner; B Greve; M Steup
Journal:  Plant Mol Biol       Date:  1995-02       Impact factor: 4.076

4.  beta-Maltose is the metabolically active anomer of maltose during transitory starch degradation.

Authors:  Sean E Weise; Kirsten S Kim; Robert P Stewart; Thomas D Sharkey
Journal:  Plant Physiol       Date:  2005-01-21       Impact factor: 8.340

5.  The role of cytosolic alpha-glucan phosphorylase in maltose metabolism and the comparison of amylomaltase in Arabidopsis and Escherichia coli.

Authors:  Yan Lu; Jon M Steichen; Jian Yao; Thomas D Sharkey
Journal:  Plant Physiol       Date:  2006-09-15       Impact factor: 8.340

6.  The role of amylomaltase in maltose metabolism in the cytosol of photosynthetic cells.

Authors:  Yan Lu; Thomas D Sharkey
Journal:  Planta       Date:  2003-10-31       Impact factor: 4.116

7.  Most of ADP x glucose linked to starch biosynthesis occurs outside the chloroplast in source leaves.

Authors:  Edurne Baroja-Fernández; Francisco José Muñoz; Aitor Zandueta-Criado; María Teresa Morán-Zorzano; Alejandro Miguel Viale; Nora Alonso-Casajús; Javier Pozueta-Romero
Journal:  Proc Natl Acad Sci U S A       Date:  2004-08-23       Impact factor: 11.205

8.  Light Alters Cytosolic and Plastidic Phosphorylase Distribution in Pearl Millet Leaves.

Authors:  KJM. Vally; M. T. Selvi; R. Sharma
Journal:  Plant Physiol       Date:  1995-10       Impact factor: 8.340

9.  Domain characterization of a 4-alpha-glucanotransferase essential for maltose metabolism in photosynthetic leaves.

Authors:  Jon M Steichen; Ryan V Petty; Thomas D Sharkey
Journal:  J Biol Chem       Date:  2008-05-22       Impact factor: 5.157

10.  Glucan phosphorylases in Vicia faba L.: cloning, structural analysis and expression patterns of cytosolic and plastidic forms in relation to starch.

Authors:  P Buchner; L Borisjuk; U Wobus
Journal:  Planta       Date:  1996       Impact factor: 4.116

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