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phosphoglucomutase/mais
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10 Ergebnisse
Inheritance, intracellular localization, and genetic variation of phosphoglucomutase isozymes in maize (Zea mays L.).
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Phosphoglucomutase (PGM; EC 2.7.5.1) isozyme variants were studied in a large number of inbred lines, crosses, and races of maize (Zea mays L.). Patterns of Mendelian inheritance demonstrated for PGM isozyme variants indicated that they are encoded by nuclear genes. Two unlinked loci, Pgml and Pgm2,
Molecular and biochemical characterization of cytosolic phosphoglucomutase in maize. Expression during development and in response to oxygen deprivation.
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Phosphoglucomutase (PGM) catalyzes the interconversion of glucose (Glc)-1- and Glc-6-phosphate in the synthesis and consumption of sucrose. We isolated two maize (Zea mays L.) cDNAs that encode PGM with 98.5% identity in their deduced amino acid sequence. Southern-blot analysis with genomic DNA from
Purification, separation and characterization of phosphoglucomutase and phosphomannomutase from maize leaves.
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Different phosphomutases-phosphoglucomutase (EC 2.7.5.1; PGM) and phosphomannomutase (EC 2.7.5.7; PMM) from maize (Zea mays L.) leaves have been purified. PGM and PMM were completely separated from each other. The purified PGM was shown to be electrophoretically homogeneous. The PGM from maize
Many maize inbreds lack an endosperm cytosolic phosphoglucomutase.
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Starch gel electrophoresis of extracts from developing maize (Zea mays L.) endosperms 22 days postpollination reveals only a single zone of phosphoglucomutase activity in the majority of the inbreds tested. The other inbreds had the expected two zones of activity. The activity that is present in all
Purification and some catalytic properties of phosphoglucomutase from maize leaves
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Phosphoglucomutase (EC 2.7.5.1, PGM) was purified to homogeneity from maize (Zea mays L.) leaves. The enzyme had specific activity 11. 7 U/mg protein and molecular mass (determined by gel-chromatography) of 133 +/- 4 kD. The molecular mass of PGM subunits determined by SDS-electrophoresis was 66 +/-
A survey for isoenzymes of glucosephosphate isomerase, phosphoglucomutase, glucose-6-phosphate dehydrogenase and 6-Phosphogluconate dehydrogenase in C3-, C 4-and crassulacean-acid-metabolism plants, and green algae.
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Two isoenzymes each of glucosephosphate isomerase (EC 5.3.1.9), phosphoglucomutase (EC 2.7.5.1), glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (EC 1.1.1.43) were separated by (NH4)2SO4 gradient solubilization and DEAE-cellulose ion-exchange chromatography from
Correlation-Based Network Analysis of Metabolite and Enzyme Profiles Reveals a Role of Citrate Biosynthesis in Modulating N and C Metabolism in Zea mays.
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To investigate the natural variability of leaf metabolism and enzymatic activity in a maize inbred population, statistical and network analyses were employed on metabolite and enzyme profiles. The test of coefficient of variation showed that sugars and amino acids displayed opposite trends in their
Enzyme activities associated with maize kernel amyloplasts.
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Activities of the enzymes of gluconeogenesis and of starch metabolism were measured in extracts of amyloplasts isolated from protoplasts derived from 14-day-old maize (Zea mays L., cv Pioneer 3780) endosperm. The enzymes triosephosphate isomerase, fructose-1,6-bisphosphate aldolase,
Response of enzymes and storage proteins of maize endosperm to nitrogen supply.
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To examine the effects of N nutrition upon endosperm development, maize (Zea mays) kernels were grown in vitro with either 0, 3.6, 7.1, 14.3, or 35.7 millimolar N. Kernels were harvested at 20 days after pollination for determination of enzyme activities and again at maturity for quantification of
Enzymes of sucrose and hexose metabolism in developing kernels of two inbreds of maize.
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Tissue distribution and activity of enzymes involved in sucrose and hexose metabolism were examined in kernels of two inbreds of maize (Zea mays L.) at progressive stages of development. Levels of sugars and starch were also quantitated throughout development. Enzyme activities studied were:
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