Literature DB >> 16668436

Changes in beta-1,3-Glucan Synthase Activity in Developing Lima Bean Plants.

W M Dugger1, R L Palmer, C C Black.   

Abstract

A plasma membrane-enriched fraction was isolated from various tissues of developing lima bean seedlings, Phaseolus lunatus var Cangreen, to study beta-1,3-glucan synthase activity changes. All tissues contained an active beta-glucan synthase, including the cotyledons that will be senescent in mature lima bean plants. Young primary leaves exhibited a very active beta-glucan synthase; but this activity dropped markedly, about fivefold, as the leaves gained weight and became photosynthetic. Some tissues, such as the hypocotyl and young stem, exhibited an increase in beta-glucan synthase activity as the tissues were growing and a decrease as the growth rate slowed. Roots exhibited a high activity early in development that only decreased slightly, about 30%, as root growth increased. Surprisingly the senescent cotyledons contained an activity equivalent to some other tissues that was maintained over our measurement time of 21 days. Perhaps this callose synthesis activity is related to translocation processes as the cotyledons transfer their reserves to the growing seedling. We concluded that beta-glucan synthase was not a good indicator of sink strength in these lima bean tissues. The plasma membrane fractions also were tested for other enzymes that might be present because an electron microscope study revealed a low contamination by other types of membranes. The membrane fractions had low but detectable activities of sucrose synthase, UDPglucose pyrophosphorylase, UDPase, alkaline invertase, and a general phosphatase; but these enzymes exhibited no consistent pattern(s) of activity change with plant development.

Entities:  

Year:  1991        PMID: 16668436      PMCID: PMC1081044          DOI: 10.1104/pp.97.2.569

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


  18 in total

1.  Modulation of Pea Membrane beta-Glucan Synthase Activity by Calcium, Polycation, Endogenous Protease, and Protease Inhibitor.

Authors:  V Girard; G Maclachlan
Journal:  Plant Physiol       Date:  1987-09       Impact factor: 8.340

2.  Uridine diphosphate glucose pyrophosphorylase from Sorghum vulgare. Purification and kinetic properties.

Authors:  G L Gustafson; J E Gander
Journal:  J Biol Chem       Date:  1972-03-10       Impact factor: 5.157

3.  Ion-exchange paper chromatography of nucleoside diphosphate sugars and related nucleotides.

Authors:  H Verachtert; S T Bass; J Wilder; R G Hansen
Journal:  Anal Biochem       Date:  1965-06       Impact factor: 3.365

4.  Characterization of Sucrolysis via the Uridine Diphosphate and Pyrophosphate-Dependent Sucrose Synthase Pathway.

Authors:  D P Xu; S J Sung; T Loboda; P P Kormanik; C C Black
Journal:  Plant Physiol       Date:  1989-06       Impact factor: 8.340

5.  UDP-Glucose: (1,3)-beta-Glucan Synthase from Daucus carota L. : Characterization, Photoaffinity Labeling, and Solubilization.

Authors:  S G Lawson; T L Mason; R D Sabin; M E Sloan; R R Drake; B E Haley; B P Wasserman
Journal:  Plant Physiol       Date:  1989-05       Impact factor: 8.340

6.  UDP-Glucose: (1-->3)-beta-Glucan Synthases from Mung Bean and Cotton: Differential Effects of Ca and Mg on Enzyme Properties and on Macromolecular Structure of the Glucan Product.

Authors:  T Hayashi; S M Read; J Bussell; M Thelen; F C Lin; R M Brown; D P Delmer
Journal:  Plant Physiol       Date:  1987-04       Impact factor: 8.340

7.  (1-->3)-beta-d-Glucan Synthase from Sugar Beet : II. Product Inhibition by UDP.

Authors:  D L Morrow; W J Lucas
Journal:  Plant Physiol       Date:  1987-07       Impact factor: 8.340

8.  Light/Dark profiles of sucrose phosphate synthase, sucrose synthase, and Acid invertase in leaves of sugar beets.

Authors:  T L Vassey
Journal:  Plant Physiol       Date:  1989-01       Impact factor: 8.340

9.  In vitro glucan synthesis by membranes of celery petioles: the role of the membrane in determining the type of linkage formed.

Authors:  S R Jacob; D H Northcote
Journal:  J Cell Sci Suppl       Date:  1985

10.  Reversible unidirectional inhibition of sucrose synthase activity by disulfides.

Authors:  H G Pontis; J R Babio; G Salerno
Journal:  Proc Natl Acad Sci U S A       Date:  1981-11       Impact factor: 11.205

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