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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.

Planta

Herbert M, Burkhard C, Schnarrenberger C.
PMID: 24317570
Planta. 1979 Jan;145(1):95-104. doi: 10.1007/BF00379933.

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 green leaves of the C3-plants spinach (Spinacia oleracea...

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Herbert M, Burkhard C, Schnarrenberger C. 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. Planta. 1979;145(1):95-104doi: 10.1007/BF00379933.
Herbert, M., Burkhard, C., & Schnarrenberger, C. (1979). 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. Planta, 145(1), 95-104. https://doi.org/10.1007/BF00379933
Herbert, M, et al. "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." Planta vol. 145,1 (1979): 95-104. doi: https://doi.org/10.1007/BF00379933
Herbert M, Burkhard C, Schnarrenberger C. 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. Planta. 1979 Jan;145(1):95-104. doi: 10.1007/BF00379933. PMID: 24317570.
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Comparative and genetic studies of isozymes in resynthesized and cultivated Brassica napus L., B. campestris L. and B. alboglabra Bailey.

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

Chen BY, Heneen WK, Simonsen V.
PMID: 24232800
Theor Appl Genet. 1989 May;77(5):673-9. doi: 10.1007/BF00261242.

Enzyme electrophoresis was used to compare newly resynthesized Brassica napus with its actual parental diploid species, B. campestris and B. alboglabra. Comparisons were also made with cultivated B. napus. Of the eight enzyme systems assayed, four were monomorphic (hexokinase,...

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Chen BY, Heneen WK, Simonsen V. Comparative and genetic studies of isozymes in resynthesized and cultivated Brassica napus L., B. campestris L. and B. alboglabra Bailey. Theor Appl Genet. 1989;77(5):673-9doi: 10.1007/BF00261242.
Chen, B. Y., Heneen, W. K., & Simonsen, V. (1989). Comparative and genetic studies of isozymes in resynthesized and cultivated Brassica napus L., B. campestris L. and B. alboglabra Bailey. TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 77(5), 673-9. https://doi.org/10.1007/BF00261242
Chen, B Y, et al. "Comparative and genetic studies of isozymes in resynthesized and cultivated Brassica napus L., B. campestris L. and B. alboglabra Bailey." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 77,5 (1989): 673-9. doi: https://doi.org/10.1007/BF00261242
Chen BY, Heneen WK, Simonsen V. Comparative and genetic studies of isozymes in resynthesized and cultivated Brassica napus L., B. campestris L. and B. alboglabra Bailey. Theor Appl Genet. 1989 May;77(5):673-9. doi: 10.1007/BF00261242. PMID: 24232800.
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Effect of exogenous lead on growth and carbon metabolism of pea (Pisum sativum L) seedlings.

Physiology and molecular biology of plants : an international journal of functional plant biology

Devi R, Munjral N, Gupta AK, Kaur N.
PMID: 24381440
Physiol Mol Biol Plants. 2013 Jan;19(1):81-9. doi: 10.1007/s12298-012-0143-5.

The present study investigated the effect of exogenous lead (Pb) on seedling growth, carbohydrate composition and vital enzymes of sucrose metabolism, starch degradation, pentose phosphate pathway and glycolysis in pea seedlings. With 0.5 mM Pb, reduction of about 50...

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Devi R, Munjral N, Gupta AK, et al. Effect of exogenous lead on growth and carbon metabolism of pea (Pisum sativum L) seedlings. Physiol Mol Biol Plants. 2013;19(1):81-9doi: 10.1007/s12298-012-0143-5.
Devi, R., Munjral, N., Gupta, A. K., & Kaur, N. (2013). Effect of exogenous lead on growth and carbon metabolism of pea (Pisum sativum L) seedlings. Physiology and molecular biology of plants : an international journal of functional plant biology, 19(1), 81-9. https://doi.org/10.1007/s12298-012-0143-5
Devi, Rachana, et al. "Effect of exogenous lead on growth and carbon metabolism of pea (Pisum sativum L) seedlings." Physiology and molecular biology of plants : an international journal of functional plant biology vol. 19,1 (2013): 81-9. doi: https://doi.org/10.1007/s12298-012-0143-5
Devi R, Munjral N, Gupta AK, Kaur N. Effect of exogenous lead on growth and carbon metabolism of pea (Pisum sativum L) seedlings. Physiol Mol Biol Plants. 2013 Jan;19(1):81-9. doi: 10.1007/s12298-012-0143-5. PMID: 24381440; PMCID: PMC3550685.
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Purification and some catalytic properties of phosphoglucomutase from maize leaves .

Biochemistry. Biokhimiia

Popova TN, Matasova LV, Lapot'ko AA.
PMID: 9668210
Biochemistry (Mosc). 1998 Jun;63(6):697-701.

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...

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Popova TN, Matasova LV, Lapot'ko AA. Purification and some catalytic properties of phosphoglucomutase from maize leaves . Biochemistry (Mosc). 1998;63(6):697-701
Popova, T. N., Matasova, L. V., & Lapot'ko, A. A. (1998). Purification and some catalytic properties of phosphoglucomutase from maize leaves . Biochemistry. Biokhimiia, 63(6), 697-701.
Popova, et al. "Purification and some catalytic properties of phosphoglucomutase from maize leaves ." Biochemistry. Biokhimiia vol. 63,6 (1998): 697-701.
Popova TN, Matasova LV, Lapot'ko AA. Purification and some catalytic properties of phosphoglucomutase from maize leaves . Biochemistry (Mosc). 1998 Jun;63(6):697-701. PMID: 9668210.
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Monogenic Recessive Mutations Causing Both Late Floral Initiation and Excess Starch Accumulation in Arabidopsis.

The Plant cell

Eimert K, Wang SM, Lue WI, Chen J.
PMID: 12242359
Plant Cell. 1995 Oct;7(10):1703-1712. doi: 10.1105/tpc.7.10.1703.

A recessive Arabidopsis mutation, carbohydrate accumulation mutant1 (cam1), which maps to position 22.8 on chromosome 3, was identified by screening leaves of ethyl methanesulfonate-mutagenized M2 plants stained with iodine for altered starch content. Increased starch content in leaves of...

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Eimert K, Wang SM, Lue WI, et al. Monogenic Recessive Mutations Causing Both Late Floral Initiation and Excess Starch Accumulation in Arabidopsis. Plant Cell. 1995;7(10):1703-1712doi: 10.1105/tpc.7.10.1703.
Eimert, K., Wang, S. M., Lue, W. I., & Chen, J. (1995). Monogenic Recessive Mutations Causing Both Late Floral Initiation and Excess Starch Accumulation in Arabidopsis. The Plant cell, 7(10), 1703-1712. https://doi.org/10.1105/tpc.7.10.1703
Eimert, K., et al. "Monogenic Recessive Mutations Causing Both Late Floral Initiation and Excess Starch Accumulation in Arabidopsis." The Plant cell vol. 7,10 (1995): 1703-1712. doi: https://doi.org/10.1105/tpc.7.10.1703
Eimert K, Wang SM, Lue WI, Chen J. Monogenic Recessive Mutations Causing Both Late Floral Initiation and Excess Starch Accumulation in Arabidopsis. Plant Cell. 1995 Oct;7(10):1703-1712. doi: 10.1105/tpc.7.10.1703. PMID: 12242359; PMCID: PMC161031.
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Wildlife genetics and disease: allozyme evolution in the wild boar (Sus scrofa) caused by a swine fever epidemy.

Genetics, selection, evolution : GSE

Lang S, Pesson B, Klein F, Schreiber A.
PMID: 14736394
Genet Sel Evol. 2000 May-Jun;32(3):303-10. doi: 10.1186/1297-9686-32-3-303.

Enzyme polymorphism at 42 loci was compared before and after a major epidemy of swine fever in wild boars from northern Vosges (France). No change was observed in the 38 monomorphic loci, but allele frequencies at the phosphoglucomutase locus...

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Lang S, Pesson B, Klein F, et al. Wildlife genetics and disease: allozyme evolution in the wild boar (Sus scrofa) caused by a swine fever epidemy. Genet Sel Evol. 2000;32(3):303-10doi: 10.1186/1297-9686-32-3-303.
Lang, S., Pesson, B., Klein, F., & Schreiber, A. (2000). Wildlife genetics and disease: allozyme evolution in the wild boar (Sus scrofa) caused by a swine fever epidemy. Genetics, selection, evolution : GSE, 32(3), 303-10. https://doi.org/10.1186/1297-9686-32-3-303
Lang, S, et al. "Wildlife genetics and disease: allozyme evolution in the wild boar (Sus scrofa) caused by a swine fever epidemy." Genetics, selection, evolution : GSE vol. 32,3 (2000): 303-10. doi: https://doi.org/10.1186/1297-9686-32-3-303
Lang S, Pesson B, Klein F, Schreiber A. Wildlife genetics and disease: allozyme evolution in the wild boar (Sus scrofa) caused by a swine fever epidemy. Genet Sel Evol. 2000 May-Jun;32(3):303-10. doi: 10.1186/1297-9686-32-3-303. PMID: 14736394; PMCID: PMC2706889.
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Comparative Studies of Phosphoglucomutase.

Science (New York, N.Y.)

Handler P, Hashimoto T, Dougherty H, Hanabusa K, Joshi JG.
PMID: 17801950
Science. 1965 Apr 30;148(3670):666. doi: 10.1126/science.148.3670.666.

No abstract available.

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Handler P, Hashimoto T, Dougherty H, et al. Comparative Studies of Phosphoglucomutase. Science. 1965;148(3670):666doi: 10.1126/science.148.3670.666.
Handler, P., Hashimoto, T., Dougherty, H., Hanabusa, K., & Joshi, J. G. (1965). Comparative Studies of Phosphoglucomutase. Science (New York, N.Y.), 148(3670), 666. https://doi.org/10.1126/science.148.3670.666
Handler, P, et al. "Comparative Studies of Phosphoglucomutase." Science (New York, N.Y.) vol. 148,3670 (1965): 666. doi: https://doi.org/10.1126/science.148.3670.666
Handler P, Hashimoto T, Dougherty H, Hanabusa K, Joshi JG. Comparative Studies of Phosphoglucomutase. Science. 1965 Apr 30;148(3670):666. doi: 10.1126/science.148.3670.666. PMID: 17801950.
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Carbon Partitioning and Growth of a Starchless Mutant of Nicotiana sylvestris.

Plant physiology

Huber SC, Hanson KR.
PMID: 16669057
Plant Physiol. 1992 Aug;99(4):1449-54. doi: 10.1104/pp.99.4.1449.

We have further characterized the photosynthetic carbohydrate metabolism and growth of a starchless mutant (NS 458) of Nicotiana sylvestris that is deficient in plastid phosphoglucomutase (Hanson KR, McHale NA [1988] Plant Physiol 88: 838-844). In general, the mutant had...

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Huber SC, Hanson KR. Carbon Partitioning and Growth of a Starchless Mutant of Nicotiana sylvestris. Plant Physiol. 1992;99(4):1449-54doi: 10.1104/pp.99.4.1449.
Huber, S. C., & Hanson, K. R. (1992). Carbon Partitioning and Growth of a Starchless Mutant of Nicotiana sylvestris. Plant physiology, 99(4), 1449-54. https://doi.org/10.1104/pp.99.4.1449
Huber, S C, and Hanson, K R. "Carbon Partitioning and Growth of a Starchless Mutant of Nicotiana sylvestris." Plant physiology vol. 99,4 (1992): 1449-54. doi: https://doi.org/10.1104/pp.99.4.1449
Huber SC, Hanson KR. Carbon Partitioning and Growth of a Starchless Mutant of Nicotiana sylvestris. Plant Physiol. 1992 Aug;99(4):1449-54. doi: 10.1104/pp.99.4.1449. PMID: 16669057; PMCID: PMC1080646.
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Enzymes of sucrose and hexose metabolism in developing kernels of two inbreds of maize.

Plant physiology

Doehlert DC, Kuo TM, Felker FC.
PMID: 16666024
Plant Physiol. 1988 Apr;86(4):1013-9. doi: 10.1104/pp.86.4.1013.

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....

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Doehlert DC, Kuo TM, Felker FC. Enzymes of sucrose and hexose metabolism in developing kernels of two inbreds of maize. Plant Physiol. 1988;86(4):1013-9doi: 10.1104/pp.86.4.1013.
Doehlert, D. C., Kuo, T. M., & Felker, F. C. (1988). Enzymes of sucrose and hexose metabolism in developing kernels of two inbreds of maize. Plant physiology, 86(4), 1013-9. https://doi.org/10.1104/pp.86.4.1013
Doehlert, D C, et al. "Enzymes of sucrose and hexose metabolism in developing kernels of two inbreds of maize." Plant physiology vol. 86,4 (1988): 1013-9. doi: https://doi.org/10.1104/pp.86.4.1013
Doehlert DC, Kuo TM, Felker FC. Enzymes of sucrose and hexose metabolism in developing kernels of two inbreds of maize. Plant Physiol. 1988 Apr;86(4):1013-9. doi: 10.1104/pp.86.4.1013. PMID: 16666024; PMCID: PMC1054620.
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Effects of cryogenic treatment on plantlet production from frozen and unfrozen date palm callus.

Plant physiology

Ulrich JM, Finkle BJ, Tisserat BH.
PMID: 16662261
Plant Physiol. 1982 Mar;69(3):624-7. doi: 10.1104/pp.69.3.624.

Embryogenic date palm (Phoenix dactylifera L. var. Medjool) callus cultures were treated with a cryoprotective mixture of polyethylene glycol (Carbowax 6000), glucose, and dimethylsulfoxide (10%/8%/10%, w/v); treated with the mixture, frozen to -196 degrees C, and then thawed; or...

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Ulrich JM, Finkle BJ, Tisserat BH. Effects of cryogenic treatment on plantlet production from frozen and unfrozen date palm callus. Plant Physiol. 1982;69(3):624-7doi: 10.1104/pp.69.3.624.
Ulrich, J. M., Finkle, B. J., & Tisserat, B. H. (1982). Effects of cryogenic treatment on plantlet production from frozen and unfrozen date palm callus. Plant physiology, 69(3), 624-7. https://doi.org/10.1104/pp.69.3.624
Ulrich, J M, et al. "Effects of cryogenic treatment on plantlet production from frozen and unfrozen date palm callus." Plant physiology vol. 69,3 (1982): 624-7. doi: https://doi.org/10.1104/pp.69.3.624
Ulrich JM, Finkle BJ, Tisserat BH. Effects of cryogenic treatment on plantlet production from frozen and unfrozen date palm callus. Plant Physiol. 1982 Mar;69(3):624-7. doi: 10.1104/pp.69.3.624. PMID: 16662261; PMCID: PMC426266.
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Effects of fructose 2,6-bisphosphate on phosphoglucomutase from plants.

Plant physiology

Carreras M, Bartrons R, Climent F, Carreras J.
PMID: 16665081
Plant Physiol. 1986 Oct;82(2):619-21. doi: 10.1104/pp.82.2.619.

Fructose 2,6-bisphosphate affects phosphoglucomutase from plant and animal sources in a similar way. As previously found with rabbit muscle phosphoglucomutase, fructose 2,6-bisphosphate cannot substitute for glucose 1,6-bisphosphate as a cofactor in the reaction catalyzed by phosphoglucomutase from potato tubers,...

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Carreras M, Bartrons R, Climent F, et al. Effects of fructose 2,6-bisphosphate on phosphoglucomutase from plants. Plant Physiol. 1986;82(2):619-21doi: 10.1104/pp.82.2.619.
Carreras, M., Bartrons, R., Climent, F., & Carreras, J. (1986). Effects of fructose 2,6-bisphosphate on phosphoglucomutase from plants. Plant physiology, 82(2), 619-21. https://doi.org/10.1104/pp.82.2.619
Carreras, M, et al. "Effects of fructose 2,6-bisphosphate on phosphoglucomutase from plants." Plant physiology vol. 82,2 (1986): 619-21. doi: https://doi.org/10.1104/pp.82.2.619
Carreras M, Bartrons R, Climent F, Carreras J. Effects of fructose 2,6-bisphosphate on phosphoglucomutase from plants. Plant Physiol. 1986 Oct;82(2):619-21. doi: 10.1104/pp.82.2.619. PMID: 16665081; PMCID: PMC1056172.
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Fructose 2,6-bisphosphate inhibition of phosphoglucomutase.

Plant physiology

Galloway CM, Dugger WM, Black CC.
PMID: 16666490
Plant Physiol. 1988 Dec;88(4):980-2. doi: 10.1104/pp.88.4.980.

Fructose 2,6-bisphosphate inhibits phosphoglucomutase noncompetitively with respect to the cofactor glucose 1,6-bisphosphate. Previous studies from our laboratory had shown that phosphoglucomutase was activated by fructose 2,6-bisphosphate in the absence of added glucose 1,6-bisphosphate. The fructose 2,6-bisphosphate activation previously reported...

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Galloway CM, Dugger WM, Black CC. Fructose 2,6-bisphosphate inhibition of phosphoglucomutase. Plant Physiol. 1988;88(4):980-2doi: 10.1104/pp.88.4.980.
Galloway, C. M., Dugger, W. M., & Black, C. C. (1988). Fructose 2,6-bisphosphate inhibition of phosphoglucomutase. Plant physiology, 88(4), 980-2. https://doi.org/10.1104/pp.88.4.980
Galloway, C M, et al. "Fructose 2,6-bisphosphate inhibition of phosphoglucomutase." Plant physiology vol. 88,4 (1988): 980-2. doi: https://doi.org/10.1104/pp.88.4.980
Galloway CM, Dugger WM, Black CC. Fructose 2,6-bisphosphate inhibition of phosphoglucomutase. Plant Physiol. 1988 Dec;88(4):980-2. doi: 10.1104/pp.88.4.980. PMID: 16666490; PMCID: PMC1055698.
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