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Showing 1 to 12 of 68 entries
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Role of ATP in nitrite reduction in roots of wheat and pea.

Planta

Dry I, Wallace W, Nicholas DJ.
PMID: 24302420
Planta. 1981 Jul;152(3):234-8. doi: 10.1007/BF00385149.

Excised wheat (Triticum aestivum L.) and field pea (Pisum arvense L.) roots, incubated under anaerobic conditions or in the presence of uncouplers of oxidative phosphorylation [2,4-dinitrophenol (DNP), carbonylcyanide-m-chlorophenylhydrazone, pentachlorophenol] accumulated nitrite as a result of an inhibition of nitrite...

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Dry I, Wallace W, Nicholas DJ. Role of ATP in nitrite reduction in roots of wheat and pea. Planta. 1981;152(3):234-8doi: 10.1007/BF00385149.
Dry, I., Wallace, W., & Nicholas, D. J. (1981). Role of ATP in nitrite reduction in roots of wheat and pea. Planta, 152(3), 234-8. https://doi.org/10.1007/BF00385149
Dry, I, et al. "Role of ATP in nitrite reduction in roots of wheat and pea." Planta vol. 152,3 (1981): 234-8. doi: https://doi.org/10.1007/BF00385149
Dry I, Wallace W, Nicholas DJ. Role of ATP in nitrite reduction in roots of wheat and pea. Planta. 1981 Jul;152(3):234-8. doi: 10.1007/BF00385149. PMID: 24302420.
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Light-regulation of enzyme activity in anacystis nidulans (Richt.).

Planta

Duggan JX, Anderson LE.
PMID: 24435997
Planta. 1975 Jan;122(3):293-7. doi: 10.1007/BF00385278.

The effect of light on the levels of activity of six enzymes which are light-modulated in higher plants was examined in the photosynthetic procaryot Anacystis nidulans. Ribulose-5-phosphate kinase (EC 2.7.1.19) was found to be light-activated in vivo and dithiothreitol-activated...

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Duggan JX, Anderson LE. Light-regulation of enzyme activity in anacystis nidulans (Richt.). Planta. 1975;122(3):293-7doi: 10.1007/BF00385278.
Duggan, J. X., & Anderson, L. E. (1975). Light-regulation of enzyme activity in anacystis nidulans (Richt.). Planta, 122(3), 293-7. https://doi.org/10.1007/BF00385278
Duggan, J X, and Anderson, L E. "Light-regulation of enzyme activity in anacystis nidulans (Richt.)." Planta vol. 122,3 (1975): 293-7. doi: https://doi.org/10.1007/BF00385278
Duggan JX, Anderson LE. Light-regulation of enzyme activity in anacystis nidulans (Richt.). Planta. 1975 Jan;122(3):293-7. doi: 10.1007/BF00385278. PMID: 24435997.
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Truncated Glycolytic System in Veillonella.

Journal of bacteriology

Rogosa M, Krichevsky MI, Bishop FS.
PMID: 16562014
J Bacteriol. 1965 Jul;90(1):164-71. doi: 10.1128/jb.90.1.164-171.1965.

Rogosa, M., (National Institutes of Health, Bethesda, Md.), M. I. Krichevsky, and F. S. Bishop. Truncated glycolytic system in Veillonella. J. Bacteriol. 90:164-171. 1965.-Intact Veillonella cells do not utilize carbohydrates for growth, nor are carbohydrates fermented. In cell extracts,...

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Rogosa M, Krichevsky MI, Bishop FS. Truncated Glycolytic System in Veillonella. J Bacteriol. 1965;90(1):164-71doi: 10.1128/jb.90.1.164-171.1965.
Rogosa, M., Krichevsky, M. I., & Bishop, F. S. (1965). Truncated Glycolytic System in Veillonella. Journal of bacteriology, 90(1), 164-71. https://doi.org/10.1128/jb.90.1.164-171.1965
Rogosa, M, et al. "Truncated Glycolytic System in Veillonella." Journal of bacteriology vol. 90,1 (1965): 164-71. doi: https://doi.org/10.1128/jb.90.1.164-171.1965
Rogosa M, Krichevsky MI, Bishop FS. Truncated Glycolytic System in Veillonella. J Bacteriol. 1965 Jul;90(1):164-71. doi: 10.1128/jb.90.1.164-171.1965. PMID: 16562014; PMCID: PMC315610.
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Isolation of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase Activity.

Journal of bacteriology

Böck A, Neidhardt FC.
PMID: 16562136
J Bacteriol. 1966 Aug;92(2):464-9. doi: 10.1128/jb.92.2.464-469.1966.

Böck, August (Purdue University, Lafayette, Ind.), and Frederick C. Neidhardt. Isolation of a mutant of Escherichia coli with a temperature-sensitive fructose-1,6-diphosphate aldolase activity. J. Bacteriol. 92:464-469. 1966.-A mutant of Escherichia coli was isolated which was able to grow in...

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Böck A, Neidhardt FC. Isolation of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase Activity. J Bacteriol. 1966;92(2):464-9doi: 10.1128/jb.92.2.464-469.1966.
Böck, A., & Neidhardt, F. C. (1966). Isolation of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase Activity. Journal of bacteriology, 92(2), 464-9. https://doi.org/10.1128/jb.92.2.464-469.1966
Böck, A, and Neidhardt, F C. "Isolation of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase Activity." Journal of bacteriology vol. 92,2 (1966): 464-9. doi: https://doi.org/10.1128/jb.92.2.464-469.1966
Böck A, Neidhardt FC. Isolation of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase Activity. J Bacteriol. 1966 Aug;92(2):464-9. doi: 10.1128/jb.92.2.464-469.1966. PMID: 16562136; PMCID: PMC276264.
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Properties of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase.

Journal of bacteriology

Böck A, Neidhardt FC.
PMID: 16562137
J Bacteriol. 1966 Aug;92(2):470-6. doi: 10.1128/jb.92.2.470-476.1966.

Böck, August (Purdue University, Lafayette, Ind.), and Frederick C. Neidhardt. Properties of a mutant of Escherichia coli with a temperature-sensitive fructose-1,6-diphosphate aldolase. J. Bacteriol. 92:470-476. 1966.-A mutant of Escherichia coli in which fructose-1,6-diphosphate aldolase functions at 30 C but...

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Böck A, Neidhardt FC. Properties of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase. J Bacteriol. 1966;92(2):470-6doi: 10.1128/jb.92.2.470-476.1966.
Böck, A., & Neidhardt, F. C. (1966). Properties of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase. Journal of bacteriology, 92(2), 470-6. https://doi.org/10.1128/jb.92.2.470-476.1966
Böck, A, and Neidhardt, F C. "Properties of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase." Journal of bacteriology vol. 92,2 (1966): 470-6. doi: https://doi.org/10.1128/jb.92.2.470-476.1966
Böck A, Neidhardt FC. Properties of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase. J Bacteriol. 1966 Aug;92(2):470-6. doi: 10.1128/jb.92.2.470-476.1966. PMID: 16562137; PMCID: PMC276265.
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Relationship between the Level of Adenine Nucleotides and the Carboxylation Activity of Illuminated Isolated Spinach Chloroplasts: A Study with Antimycin A.

Plant physiology

Miginiac-Maslow M, Champigny ML.
PMID: 16658804
Plant Physiol. 1974 Jun;53(6):856-62. doi: 10.1104/pp.53.6.856.

The changes in the levels of intact spinach (Spinacia oleracea L.) chloroplast adenine nucleotides during the time course of light-dependent CO(2) fixation were determined with respect to the effect of antimycin A. This study demonstrated that antimycin A lowered...

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Miginiac-Maslow M, Champigny ML. Relationship between the Level of Adenine Nucleotides and the Carboxylation Activity of Illuminated Isolated Spinach Chloroplasts: A Study with Antimycin A. Plant Physiol. 1974;53(6):856-62doi: 10.1104/pp.53.6.856.
Miginiac-Maslow, M., & Champigny, M. L. (1974). Relationship between the Level of Adenine Nucleotides and the Carboxylation Activity of Illuminated Isolated Spinach Chloroplasts: A Study with Antimycin A. Plant physiology, 53(6), 856-62. https://doi.org/10.1104/pp.53.6.856
Miginiac-Maslow, M, and Champigny, M L. "Relationship between the Level of Adenine Nucleotides and the Carboxylation Activity of Illuminated Isolated Spinach Chloroplasts: A Study with Antimycin A." Plant physiology vol. 53,6 (1974): 856-62. doi: https://doi.org/10.1104/pp.53.6.856
Miginiac-Maslow M, Champigny ML. Relationship between the Level of Adenine Nucleotides and the Carboxylation Activity of Illuminated Isolated Spinach Chloroplasts: A Study with Antimycin A. Plant Physiol. 1974 Jun;53(6):856-62. doi: 10.1104/pp.53.6.856. PMID: 16658804; PMCID: PMC541462.
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Photosynthetic enhancement studied in intact spinach chloroplasts.

Plant physiology

Peavey DG, Gibbs M.
PMID: 16659171
Plant Physiol. 1975 May;55(5):799-802. doi: 10.1104/pp.55.5.799.

The Emerson enhancement effect was evaluated in the intact spinach (Spinacia oleracea var. Long Standing Bloomsdale) chloroplast by monitoring the uptake of (14)CO(2) during illumination by 640 nm and 720 nm lights. Low levels (about 10 mum) of fructose...

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Peavey DG, Gibbs M. Photosynthetic enhancement studied in intact spinach chloroplasts. Plant Physiol. 1975;55(5):799-802doi: 10.1104/pp.55.5.799.
Peavey, D. G., & Gibbs, M. (1975). Photosynthetic enhancement studied in intact spinach chloroplasts. Plant physiology, 55(5), 799-802. https://doi.org/10.1104/pp.55.5.799
Peavey, D G, and Gibbs, M. "Photosynthetic enhancement studied in intact spinach chloroplasts." Plant physiology vol. 55,5 (1975): 799-802. doi: https://doi.org/10.1104/pp.55.5.799
Peavey DG, Gibbs M. Photosynthetic enhancement studied in intact spinach chloroplasts. Plant Physiol. 1975 May;55(5):799-802. doi: 10.1104/pp.55.5.799. PMID: 16659171; PMCID: PMC541713.
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Level of photosynthetic intermediates in isolated spinach chloroplasts.

Plant physiology

Latzko E, Gibbs M.
PMID: 16657074
Plant Physiol. 1969 Mar;44(3):396-402. doi: 10.1104/pp.44.3.396.

The level of intermediates of the photosynthetic carbon cycle was measured in intact spinach chloroplasts in an attempt to determine the cause of the induction lag in CO(2) assimilation. In addition, transient changes in the level of the intermediates...

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Latzko E, Gibbs M. Level of photosynthetic intermediates in isolated spinach chloroplasts. Plant Physiol. 1969;44(3):396-402doi: 10.1104/pp.44.3.396.
Latzko, E., & Gibbs, M. (1969). Level of photosynthetic intermediates in isolated spinach chloroplasts. Plant physiology, 44(3), 396-402. https://doi.org/10.1104/pp.44.3.396
Latzko, E, and Gibbs, M. "Level of photosynthetic intermediates in isolated spinach chloroplasts." Plant physiology vol. 44,3 (1969): 396-402. doi: https://doi.org/10.1104/pp.44.3.396
Latzko E, Gibbs M. Level of photosynthetic intermediates in isolated spinach chloroplasts. Plant Physiol. 1969 Mar;44(3):396-402. doi: 10.1104/pp.44.3.396. PMID: 16657074; PMCID: PMC396097.
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Regulation of Photosynthetic Capacity in Chlamydomonas mundana.

Plant physiology

Russell GK, Gibbs M.
PMID: 16656335
Plant Physiol. 1966 May;41(5):885-90. doi: 10.1104/pp.41.5.885.

A regulatory system has been described in the obligately phototrophic green alga Chlamydomonas mundana. Cells grown in acetate media are unable to fix carbon dioxide in the light but carry out a photoassimilation of acetate to carbohydrate: cells cultured...

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Russell GK, Gibbs M. Regulation of Photosynthetic Capacity in Chlamydomonas mundana. Plant Physiol. 1966;41(5):885-90doi: 10.1104/pp.41.5.885.
Russell, G. K., & Gibbs, M. (1966). Regulation of Photosynthetic Capacity in Chlamydomonas mundana. Plant physiology, 41(5), 885-90. https://doi.org/10.1104/pp.41.5.885
Russell, G K, and Gibbs, M. "Regulation of Photosynthetic Capacity in Chlamydomonas mundana." Plant physiology vol. 41,5 (1966): 885-90. doi: https://doi.org/10.1104/pp.41.5.885
Russell GK, Gibbs M. Regulation of Photosynthetic Capacity in Chlamydomonas mundana. Plant Physiol. 1966 May;41(5):885-90. doi: 10.1104/pp.41.5.885. PMID: 16656335; PMCID: PMC1086441.
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Enzymatic production of fructose 1,6-diphosphate using crude cell extract of Bacillus stearothermophilus.

Journal of bioscience and bioengineering

Widjaja A, Yasuda M, Ogino H, Nakajima H, Ishikawa H.
PMID: 16232540
J Biosci Bioeng. 1999;87(5):693-6. doi: 10.1016/s1389-1723(99)80136-4.

The enzymatic production of fructose 1,6-diphosphate (FDP) from glucose was performed in a batch reactor and a semibatch reactor using the crude cell extract of Bacillus stearothermophilus which contains all four enzymes required for the synthesis. The experimental results...

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Widjaja A, Yasuda M, Ogino H, et al. Enzymatic production of fructose 1,6-diphosphate using crude cell extract of Bacillus stearothermophilus. J Biosci Bioeng. 1999;87(5):693-6doi: 10.1016/s1389-1723(99)80136-4.
Widjaja, A., Yasuda, M., Ogino, H., Nakajima, H., & Ishikawa, H. (1999). Enzymatic production of fructose 1,6-diphosphate using crude cell extract of Bacillus stearothermophilus. Journal of bioscience and bioengineering, 87(5), 693-6. https://doi.org/10.1016/s1389-1723(99)80136-4
Widjaja, A, et al. "Enzymatic production of fructose 1,6-diphosphate using crude cell extract of Bacillus stearothermophilus." Journal of bioscience and bioengineering vol. 87,5 (1999): 693-6. doi: https://doi.org/10.1016/s1389-1723(99)80136-4
Widjaja A, Yasuda M, Ogino H, Nakajima H, Ishikawa H. Enzymatic production of fructose 1,6-diphosphate using crude cell extract of Bacillus stearothermophilus. J Biosci Bioeng. 1999;87(5):693-6. doi: 10.1016/s1389-1723(99)80136-4. PMID: 16232540.
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Light-induced Enzyme Formation in a Chlorophyll-less Mutant of Euglena gracilis.

Plant physiology

Russell GK, Draffan AG.
PMID: 16660582
Plant Physiol. 1978 Nov;62(5):678-82. doi: 10.1104/pp.62.5.678.

A mutant strain, Y(9), of Euglena gracilis strain Z that is unable to produce protochlorophyll or chlorophyll has been isolated following treatment of wild type cells with nalidixic acid. Dark-grown cells of the mutant contain proplastids that show only...

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Russell GK, Draffan AG. Light-induced Enzyme Formation in a Chlorophyll-less Mutant of Euglena gracilis. Plant Physiol. 1978;62(5):678-82doi: 10.1104/pp.62.5.678.
Russell, G. K., & Draffan, A. G. (1978). Light-induced Enzyme Formation in a Chlorophyll-less Mutant of Euglena gracilis. Plant physiology, 62(5), 678-82. https://doi.org/10.1104/pp.62.5.678
Russell, G K, and Draffan, A G. "Light-induced Enzyme Formation in a Chlorophyll-less Mutant of Euglena gracilis." Plant physiology vol. 62,5 (1978): 678-82. doi: https://doi.org/10.1104/pp.62.5.678
Russell GK, Draffan AG. Light-induced Enzyme Formation in a Chlorophyll-less Mutant of Euglena gracilis. Plant Physiol. 1978 Nov;62(5):678-82. doi: 10.1104/pp.62.5.678. PMID: 16660582; PMCID: PMC1092197.
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Bioconversion of lactose/whey to fructose diphosphate with recombinant saccharomyces cerevisiae cells.

Biotechnology and bioengineering

Compagno C, Tura A, Ranzi BM, Martegani E.
PMID: 18613026
Biotechnol Bioeng. 1993 Jul;42(3):398-400. doi: 10.1002/bit.260420319.

Genetically engineered Saccharomyces cerevisiae strains that express Escherichia coli beta-galactosidase gene are able to bioconvert lactose or whey into fructose-1,6-diphosphate (FDP). High FDP yields from whey were obtained with an appropriate ratio between cell concentration and inorganic phosphate. The...

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Compagno C, Tura A, Ranzi BM, et al. Bioconversion of lactose/whey to fructose diphosphate with recombinant saccharomyces cerevisiae cells. Biotechnol Bioeng. 1993;42(3):398-400doi: 10.1002/bit.260420319.
Compagno, C., Tura, A., Ranzi, B. M., & Martegani, E. (1993). Bioconversion of lactose/whey to fructose diphosphate with recombinant saccharomyces cerevisiae cells. Biotechnology and bioengineering, 42(3), 398-400. https://doi.org/10.1002/bit.260420319
Compagno, C, et al. "Bioconversion of lactose/whey to fructose diphosphate with recombinant saccharomyces cerevisiae cells." Biotechnology and bioengineering vol. 42,3 (1993): 398-400. doi: https://doi.org/10.1002/bit.260420319
Compagno C, Tura A, Ranzi BM, Martegani E. Bioconversion of lactose/whey to fructose diphosphate with recombinant saccharomyces cerevisiae cells. Biotechnol Bioeng. 1993 Jul;42(3):398-400. doi: 10.1002/bit.260420319. PMID: 18613026.
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Showing 1 to 12 of 68 entries