Results 251 to 260 of about 60,616 (293)

Sheep kidney phosphoenolpyruvate carboxylase purification and properties

Biochimica et Biophysica Acta (BBA) - Enzymology, 1972
Phosphoenolpyruvate carboxylase (GTP: oxaloacetate carboxy-lase (transphosphorylating), EC 4.1.1.32) has been purified and obtained in a homogeneous form from sheep kidney cortex mitochondria. The purification procedure involved extraction of the freeze-dried mitochondria, (NH4)2SO4 fractionation, Sephadex G-100 gel filtration and ion-exchange ...
R.J. Barns, D.B. Keech
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Improvement of the photosynthetic characteristics of transgenic wheat plants by transformation with the maize C4 phosphoenolpyruvate carboxylase gene

, 2012
With 7 figures and 2 tables Abstract Attempts have been made to transform C3 crops with C4 genes to improve the photosynthetic rate of C3 plants. In our study, a full-length cDNA for phosphoenolpyruvate carboxylase gene (pepc) was isolated from
Lin Hu, Yan Li, Weigang Xu, Qingchen Zhang, Lei Zhang, Qi Xueli, Haibin Dong   +6 more
semanticscholar   +1 more source

A microtiter plate-based assay for phosphoenolpyruvate carboxylase

Analytical Biochemistry, 1990
A sensitive, quantitative assay for phosphenolpyruvate carboxylase which utilizes microtiter plates is described. The assay depends upon the production of a colored compound in the reaction between oxaloacetate, the product of the phosphoenolpyruvate reaction, and the dye Fast Violet B.
Stephen P. Slocombe, Stephen P. Slocombe, Garry C. Whitelam, Garry C. Whitelam, Raymond A. McKee, Raymond A. McKee, William Cockburn, William Cockburn   +7 more
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Phosphoenolpyruvate carboxylase and ammonium metabolism in oral streptococci

Archives of Oral Biology, 1973
Abstract Oral streptococci were grown in media which provide various nitrogen sources. Ammonium fixation was studied in cell-free extracts of the cells. Carbon dioxide fixation was studied in washed intact cells and in crude and partially purified extracts of the cells.
Jan Carlsson, Tadashi Yamada
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Phosphoenolpyruvate Carboxylase

Research Methods of Environmental Physiology in Aquatic Sciences, 2020
Fan Hu, Hanhua Hu
semanticscholar   +2 more sources

Quantitative Immunochemistry of Plant Phosphoenolpyruvate Carboxylases

1986
Since its discovery (Bandurski and Greiner 1953) phosphoenolpyruvate carboxylase (PEPC, EC 4.1.1.31) has attracted increasing interest among plant scientists. The enzyme catalyses the reaction of CO3H− and phosphoenolpyruvate to produce oxaloacetate, immediately reduced to form malate; this latter can be oxidatively decarboxylated by NADP malic enzyme,
J. Brulfert, J. Vidal
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Effects of pH on inactivation of maize phosphoenolpyruvate carboxylase

Archives of Biochemistry and Biophysics, 1990
Maize leaf phosphoenolpyruvate carboxylase (PEPC) is inactivated by incubation at pH's above neutrality. Both the amount and the rapidity of inactivation increase as the pH rises. The presence of phosphoenolpyruvate (PEP), malate, glucose 6-phosphate and dithiothreitol in the incubation medium give protection to the enzyme.
Randolph T. Wedding, M. K. Black
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On the cellular localization of phosphoenolpyruvate carboxylase in Sorghum leaves

Planta, 1981
The localization of phosphoenol pyruvate carboxylase (EC 4.1.1.3.1.) in the leaf cells of Sorghum vulgare was investigated by using three techniques: the conventional aqueous and non aqueous methods gave conflicting results; the immunocytochemical techniques clearly showed that the enzyme is predominantly located in the cytoplasm of mesophyll cells.
Jean Vidal, Pierre Gadal, Arlette Burlet, Catherine Perrot   +3 more
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Regulation of soybean nodule phosphoenolpyruvate carboxylase in vivo

Physiologia Plantarum, 1996
The sensitivity of soybean (Glycine max L. Merr, cv. PS47) nodule phosphoenolpyruvate carboxylase (PEPC; EC 4.1.1.31) to inhibition by L‐malate in vitro increased when well‐nodulated plants were subjected to decapitation (shoot removal). There was no effect of decapitation on the apparent Km of the enzyme for its substrate PEP but the I50 (L‐malate ...
Carol Wadham, Kathryn A. Schuller, Heike Winter   +2 more
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Comparative studies of coupled assays for phosphoenolpyruvate carboxylase

Physiologia Plantarum, 1994
Phosphoenolpyruvate carboxylase (PEPC) from higher plants is usually assayed by using malate dehydrogenase (MDH) as a coupling enzyme. To avoid erroneous readings caused by metal ions, which convert oxaloacetate (OAA) to pyruvate, lactic dehydrogenase can be included. Reporting the total NADH used by both coupling enzymes gives the total OAA production.
Randolph T. Wedding, Katie Kline
openaire   +2 more sources