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Article
Molecular regulation of starch metabolism
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Article
Sequence variation, differential expression, and divergent evolution in starch-related genes among accessions of Arabidopsis thaliana
Transitory starch metabolism is a nonlinear and highly regulated process. It originated very early in the evolution of chloroplast-containing cells and is largely based on a mosaic of genes derived from either...
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Chapter
Starch Degradation
Degradation of starch (and of glycogen as well) converts carbohydrates accumulated as metabolically inert storage products back into forms that are usable for various biosynthetic and catabolic routes. Starch ...
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Article
Open AccessVMP1-deficient Chlamydomonas exhibits severely aberrant cell morphology and disrupted cytokinesis
The versatile Vacuole Membrane Protein 1 (VMP1) has been previously investigated in six species. It has been shown to be essential in macroautophagy, where it takes part in autophagy initiation. In addition, V...
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Article
Open AccessIntraspecific sequence variation and differential expression in starch synthase genes of Arabidopsis thaliana
Natural accessions of Arabidopsis thaliana are a well-known system to measure levels of intraspecific genetic variation. Leaf starch content correlates negatively with biomass. Starch is synthesized by the coordi...
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Article
Determination of the starch-phosphorylating enzyme activity in plant extracts
For quantification of α-glucan, water dikinase (GWD) activity in crude extracts of plant tissues a radio-labeling assay was established that uses soluble starch and 33P-labeled ATP as phosphate acceptor and dono...
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Article
Plastidic (Pho1-type) phosphorylase isoforms in potato (Solanum tuberosum L.) plants: expression analysis and immunochemical characterization
Higher plants contain two types of phosphorylase (EC 2.4.1.1). One type is plastidic (Pho1) and the other resides in the cytosol (Pho2). For Solanum tuberosum L., two highly homologous Pho1-type sequences (desig...
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Article
Analysis of phloem protein patterns from different organs of Cucurbita maxima Duch. by matrix-assisted laser desorption/ionization time of flight mass spectroscopy combined with sodium dodecyl sulfate-polyacrylamide gel electrophoresis
Sieve tubes mediate the long-distance transport of nutrients and signals between source and sink organs of plants. To detect mobile phloem proteins that are differentially distributed in source and sink organ...
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Article
Induction of genes encoding plastidic phosphorylase from spinach (Spinacia oleracea L.) and potato (Solanum tuberosum L.) by exogenously supplied carbohydrates in excised leaf discs
A full-length cDNA encoding plastidic phosphorylase (Pho1, EC 2.4.1.1) from spinach (Spinacia oleracea L.) has been isolated. Analysis of the deduced protein sequence revealed considerable homologies with the cor...
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Article
A second L-type isozyme of potato glucan phosphorylase: cloning, antisense inhibition and expression analysis
In potato tubers two starch phosphorylase isozymes, types L and H, have been described and are believed to be responsible for the complete starch breakdown in this tissue. Type L has been localized in amylopla...
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Article
Glucan-phosphorylase forms in cotyledons of Pisum sativum L.: Localization, developmental change, in-vitro translation, and processing
The occurrence, location, and biosynthesis of glucan-phosphorylase (EC 2.4.1.1) isoenzymes were studied in cotyledons of develo** or germinating seeds of Pisum sativum L. Type-I and type-II isoenzymes were dete...
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Article
Multiplicity of soluble glucan-synthase activity in spinach leaves: Enzyme pattern and intracellular location
Buffer-extractable proteins from leaves of Spinacia oleracea L. were separated by non-denaturing polyacrylamide gel electrophoresis. Gels were stained for adenosine diphosphoglucose (ADPglucose)-dependent glucan-...
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Chapter
In-Vitro Translation and Processing of Compartment-Specific Glucan Phosphorylase Isozymes from Pisum Sativum L.
Glucan phosphorylase (1,4 α-D-glucan: orthophosphate α-D-glucosyl-transferase, E.C. 2.4.1.1) catalyzes the reversible transfer of a glucosyl residue between α-D-glucose-l-phosphate and a non-reducing end of an α-...
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Chapter
A Soluble Polysaccharide Fraction from Higher Plants: A Possible Physiological Substrate of the Cytosolic Phosphorylase Isozyme
In higher plants several λ-glucan metabolizing enzymes occur as plastid- and cytosol-specific isozymes (1,2). The dual intracellular location of these enzyme activities suggests that both the plastidic and the...
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Chapter
Compartment-Specific Phosphorylase Forms from Higher Plants
In the highly compartmented plant cell many reactions of carbohydrate and nitrogen metabolism occur in more than one compartment. These reactions are usually catalyzed by compartment-specific enzyme forms whic...
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Article
Electrophoretic and chromatographic separation of two fructose-1,6-bisphosphatase forms from Synechococcus leopoliensix
d-Fructose-1,6-bisphosphatase (EC 3.1.3.11) activity in crude extracts of the blue-green alga Synechococcus leopoliensis (Anacystis nidulans) has been investigated using high resolving electrophoretic and chroma...
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Chapter
Carbon Metabolism and Malate Formation in the CAM Plant Aloe arborescens
Nocturnal CO2-fixation in plants exhibiting Crassulacean Acid Metabolism (CAM) requires a supply of the acceptor phosphoenolpyruvate (PEP) from a carbon reservoir. Because this carbon source is degraded during th...
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Article
In-vitro degradation of starch granules isolated from spinach chloroplasts
The initial reactions of transitory starch degradation in Spinacia oleracea L. were investigated using an in-vitro system composed of native chloroplast starch granules, purified chloroplast and non-chloroplast f...
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Article
Mode of glucan degradation by purified phosphorylase forms from spinach leaves
The glucan specifity of the purified chloroplast and non-chloroplast forms of α-1,4-glucan phosphorylase (EC 2.4.1.1) from spinach leaves (Steup and E. Latzko (1979), Planta 145, 69–75) was investigated. Phosphor...
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Article
Purification of a non-chloroplastic α-glucan phosphorylase from spinach leaves
The non-chloroplastic α-glucan phosphorylase (EC 2.4.1.1) from spinach leaves has been purified to homogeneity as revealed by dodecylsulfate gel electrophoresis. Both purification and separation from the chlor...
