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Extended theory of polarized fluorescence for uniaxial orientation and non-coinciding absorption and emission vectors.

European journal of biochemistry

Rupprecht A.
PMID: 5823106
Eur J Biochem. 1969 Sep;10(2):297-301. doi: 10.1111/j.1432-1033.1969.tb00689.x.
Free Article

No abstract available.

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Rupprecht A. Extended theory of polarized fluorescence for uniaxial orientation and non-coinciding absorption and emission vectors. Eur J Biochem. 1969;10(2):297-301doi: 10.1111/j.1432-1033.1969.tb00689.x.
Rupprecht, A. (1969). Extended theory of polarized fluorescence for uniaxial orientation and non-coinciding absorption and emission vectors. European journal of biochemistry, 10(2), 297-301. https://doi.org/10.1111/j.1432-1033.1969.tb00689.x
Rupprecht, A. "Extended theory of polarized fluorescence for uniaxial orientation and non-coinciding absorption and emission vectors." European journal of biochemistry vol. 10,2 (1969): 297-301. doi: https://doi.org/10.1111/j.1432-1033.1969.tb00689.x
Rupprecht A. Extended theory of polarized fluorescence for uniaxial orientation and non-coinciding absorption and emission vectors. Eur J Biochem. 1969 Sep;10(2):297-301. doi: 10.1111/j.1432-1033.1969.tb00689.x. PMID: 5823106.
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Identification of an NADP/thioredoxin system in Chlamydomonas reinhardtii.

Planta

Huppe HC, Picaud A, Buchanan BB, Miginiac-Maslow M.
PMID: 24186583
Planta. 1991 Dec;186(1):115-21. doi: 10.1007/BF00201506.

The protein components of the NADP/thioredoxin system, NADP-thioredoxin reductase (NTR) and thioredoxin h, have been purified and characterized from the green alga, Chlamydomonas reinhardtii. The analysis of this system confirms that photoautotrophic Chlamydomonas cells resemble leaves in having both...

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Huppe HC, Picaud A, Buchanan BB, et al. Identification of an NADP/thioredoxin system in Chlamydomonas reinhardtii. Planta. 1991;186(1):115-21doi: 10.1007/BF00201506.
Huppe, H. C., Picaud, A., Buchanan, B. B., & Miginiac-Maslow, M. (1991). Identification of an NADP/thioredoxin system in Chlamydomonas reinhardtii. Planta, 186(1), 115-21. https://doi.org/10.1007/BF00201506
Huppe, H C, et al. "Identification of an NADP/thioredoxin system in Chlamydomonas reinhardtii." Planta vol. 186,1 (1991): 115-21. doi: https://doi.org/10.1007/BF00201506
Huppe HC, Picaud A, Buchanan BB, Miginiac-Maslow M. Identification of an NADP/thioredoxin system in Chlamydomonas reinhardtii. Planta. 1991 Dec;186(1):115-21. doi: 10.1007/BF00201506. PMID: 24186583.
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Model of the Second Most Abundant Cisplatin-DNA Cross-Link: X-ray Crystal Structure and Conformational Analysis of cis-[(NH(3))(2)Pt(9-MeA-N7)(9-EtGH-N7)](NO(3)).2H(2)O (9-MeA = 9-Methyladenine; 9-EtGH = 9-Ethylguanine).

Inorganic chemistry

Schröder G, Kozelka J, Sabat M, Fouchet MH, Beyerle-Pfnür R, Lippert B.
PMID: 11666386
Inorg Chem. 1996 Mar 13;35(6):1647-1652. doi: 10.1021/ic950754s.

A model compound of the second most abundant DNA adduct of the antitumor agent cisplatin has been synthesized and structurally and spectroscopically characterized and its conformational behavior examined: cis-[(NH(3))(2)Pt(9-MeA-N7)(9-EtGH-N7)](NO(3))(2).2H(2)O (9-MeA = 9-methyladenine; 9-EtGH = 9-ethylguanine) crystallizes in the monoclinic...

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Schröder G, Kozelka J, Sabat M, et al. Model of the Second Most Abundant Cisplatin-DNA Cross-Link: X-ray Crystal Structure and Conformational Analysis of cis-[(NH(3))(2)Pt(9-MeA-N7)(9-EtGH-N7)](NO(3)).2H(2)O (9-MeA = 9-Methyladenine; 9-EtGH = 9-Ethylguanine). Inorg Chem. 1996;35(6):1647-1652doi: 10.1021/ic950754s.
Schröder, G., Kozelka, J., Sabat, M., Fouchet, M. H., Beyerle-Pfnür, R., & Lippert, B. (1996). Model of the Second Most Abundant Cisplatin-DNA Cross-Link: X-ray Crystal Structure and Conformational Analysis of cis-[(NH(3))(2)Pt(9-MeA-N7)(9-EtGH-N7)](NO(3)).2H(2)O (9-MeA = 9-Methyladenine; 9-EtGH = 9-Ethylguanine). Inorganic chemistry, 35(6), 1647-1652. https://doi.org/10.1021/ic950754s
Schröder, Guy, et al. "Model of the Second Most Abundant Cisplatin-DNA Cross-Link: X-ray Crystal Structure and Conformational Analysis of cis-[(NH(3))(2)Pt(9-MeA-N7)(9-EtGH-N7)](NO(3)).2H(2)O (9-MeA = 9-Methyladenine; 9-EtGH = 9-Ethylguanine)." Inorganic chemistry vol. 35,6 (1996): 1647-1652. doi: https://doi.org/10.1021/ic950754s
Schröder G, Kozelka J, Sabat M, Fouchet MH, Beyerle-Pfnür R, Lippert B. Model of the Second Most Abundant Cisplatin-DNA Cross-Link: X-ray Crystal Structure and Conformational Analysis of cis-[(NH(3))(2)Pt(9-MeA-N7)(9-EtGH-N7)](NO(3)).2H(2)O (9-MeA = 9-Methyladenine; 9-EtGH = 9-Ethylguanine). Inorg Chem. 1996 Mar 13;35(6):1647-1652. doi: 10.1021/ic950754s. PMID: 11666386.
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FEBS in the new millennium.

European journal of biochemistry

Celis JE.
PMID: 10951181
Eur J Biochem. 2000 Sep;267(17):5267. doi: 10.1046/j.1432-1327.2000.01689.x.

No abstract available.

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Celis JE. FEBS in the new millennium. Eur J Biochem. 2000;267(17):5267doi: 10.1046/j.1432-1327.2000.01689.x.
Celis, J. E. (2000). FEBS in the new millennium. European journal of biochemistry, 267(17), 5267. https://doi.org/10.1046/j.1432-1327.2000.01689.x
Celis. "FEBS in the new millennium." European journal of biochemistry vol. 267,17 (2000): 5267. doi: https://doi.org/10.1046/j.1432-1327.2000.01689.x
Celis JE. FEBS in the new millennium. Eur J Biochem. 2000 Sep;267(17):5267. doi: 10.1046/j.1432-1327.2000.01689.x. PMID: 10951181.
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Molecular cloning of tomato pectin methylesterase gene and its expression in rutgers, ripening inhibitor, nonripening, and never ripe tomato fruits.

Plant physiology

Harriman RW, Tieman DM, Handa AK.
PMID: 16668419
Plant Physiol. 1991 Sep;97(1):80-7. doi: 10.1104/pp.97.1.80.

We have purified pectin methylesterase (PME; EC 3.1.11) from mature green (MG) tomato (Lycopersicon esculentum Mill. cv Rutgers) pericarp to an apparent homogeneity, raised antibodies to the purified protein, and isolated a PME cDNA clone from a lambdagtll expression...

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Harriman RW, Tieman DM, Handa AK. Molecular cloning of tomato pectin methylesterase gene and its expression in rutgers, ripening inhibitor, nonripening, and never ripe tomato fruits. Plant Physiol. 1991;97(1):80-7doi: 10.1104/pp.97.1.80.
Harriman, R. W., Tieman, D. M., & Handa, A. K. (1991). Molecular cloning of tomato pectin methylesterase gene and its expression in rutgers, ripening inhibitor, nonripening, and never ripe tomato fruits. Plant physiology, 97(1), 80-7. https://doi.org/10.1104/pp.97.1.80
Harriman, R W, et al. "Molecular cloning of tomato pectin methylesterase gene and its expression in rutgers, ripening inhibitor, nonripening, and never ripe tomato fruits." Plant physiology vol. 97,1 (1991): 80-7. doi: https://doi.org/10.1104/pp.97.1.80
Harriman RW, Tieman DM, Handa AK. Molecular cloning of tomato pectin methylesterase gene and its expression in rutgers, ripening inhibitor, nonripening, and never ripe tomato fruits. Plant Physiol. 1991 Sep;97(1):80-7. doi: 10.1104/pp.97.1.80. PMID: 16668419; PMCID: PMC1080966.
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Isolation and characterization of an alkaline phosphatase from pea thylakoids.

Plant physiology

Kieleczawa J, Coughlan SJ, Hind G.
PMID: 16668967
Plant Physiol. 1992 Jul;99(3):1029-36. doi: 10.1104/pp.99.3.1029.

Endogenous dephosphorylation of the light-harvesting chlorophyll-protein complex of photosystem II in pea (Pisum sativum, L. cv Progress 9) thylakoids drives the state 2 to state 1 transition; the responsible enzyme is a thylakoid-bound, fluoride-sensitive phosphatase with a pH optimum...

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Kieleczawa J, Coughlan SJ, Hind G. Isolation and characterization of an alkaline phosphatase from pea thylakoids. Plant Physiol. 1992;99(3):1029-36doi: 10.1104/pp.99.3.1029.
Kieleczawa, J., Coughlan, S. J., & Hind, G. (1992). Isolation and characterization of an alkaline phosphatase from pea thylakoids. Plant physiology, 99(3), 1029-36. https://doi.org/10.1104/pp.99.3.1029
Kieleczawa, J, et al. "Isolation and characterization of an alkaline phosphatase from pea thylakoids." Plant physiology vol. 99,3 (1992): 1029-36. doi: https://doi.org/10.1104/pp.99.3.1029
Kieleczawa J, Coughlan SJ, Hind G. Isolation and characterization of an alkaline phosphatase from pea thylakoids. Plant Physiol. 1992 Jul;99(3):1029-36. doi: 10.1104/pp.99.3.1029. PMID: 16668967; PMCID: PMC1080580.
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Regulation of vacuolar h-pyrophosphatase by free calcium : a reaction kinetic analysis.

Plant physiology

Rea PA, Britten CJ, Jennings IR, Calvert CM, Skiera LA, Leigh RA, Sanders D.
PMID: 16653187
Plant Physiol. 1992 Dec;100(4):1706-15. doi: 10.1104/pp.100.4.1706.

The H(+)-translocating inorganic pyrophosphatase (H(+)-PPase) associated with vesicles of the vacuolar membrane (tonoplast) isolated from beet (Beta vulgaris L.) is subject to direct inhibition by Ca(2+) and a number of other divalent cations (Co(2+), Mn(2+), Zn(2+)). By contrast, the...

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Rea PA, Britten CJ, Jennings IR, et al. Regulation of vacuolar h-pyrophosphatase by free calcium : a reaction kinetic analysis. Plant Physiol. 1992;100(4):1706-15doi: 10.1104/pp.100.4.1706.
Rea, P. A., Britten, C. J., Jennings, I. R., Calvert, C. M., Skiera, L. A., Leigh, R. A., & Sanders, D. (1992). Regulation of vacuolar h-pyrophosphatase by free calcium : a reaction kinetic analysis. Plant physiology, 100(4), 1706-15. https://doi.org/10.1104/pp.100.4.1706
Rea, P A, et al. "Regulation of vacuolar h-pyrophosphatase by free calcium : a reaction kinetic analysis." Plant physiology vol. 100,4 (1992): 1706-15. doi: https://doi.org/10.1104/pp.100.4.1706
Rea PA, Britten CJ, Jennings IR, Calvert CM, Skiera LA, Leigh RA, Sanders D. Regulation of vacuolar h-pyrophosphatase by free calcium : a reaction kinetic analysis. Plant Physiol. 1992 Dec;100(4):1706-15. doi: 10.1104/pp.100.4.1706. PMID: 16653187; PMCID: PMC1075854.
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First-order irreversible thermodynamic approach to a simple energy converter.

Physical review. E, Statistical, nonlinear, and soft matter physics

Arias-Hernandez LA, Angulo-Brown F, Paez-Hernandez RT.
PMID: 18351834
Phys Rev E Stat Nonlin Soft Matter Phys. 2008 Jan;77(1):011123. doi: 10.1103/PhysRevE.77.011123. Epub 2008 Jan 28.

Several authors have shown that dissipative thermal cycle models based on finite-time thermodynamics exhibit loop-shaped curves of power output versus efficiency, such as it occurs with actual dissipative thermal engines. Within the context of first-order irreversible thermodynamics (FOIT), in...

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Arias-Hernandez LA, Angulo-Brown F, Paez-Hernandez RT. First-order irreversible thermodynamic approach to a simple energy converter. Phys Rev E Stat Nonlin Soft Matter Phys. 2008;77(1):011123doi: 10.1103/PhysRevE.77.011123.
Arias-Hernandez, L. A., Angulo-Brown, F., & Paez-Hernandez, R. T. (2008). First-order irreversible thermodynamic approach to a simple energy converter. Physical review. E, Statistical, nonlinear, and soft matter physics, 77(1), 011123. https://doi.org/10.1103/PhysRevE.77.011123
Arias-Hernandez, L A, et al. "First-order irreversible thermodynamic approach to a simple energy converter." Physical review. E, Statistical, nonlinear, and soft matter physics vol. 77,1 (2008): 011123. doi: https://doi.org/10.1103/PhysRevE.77.011123
Arias-Hernandez LA, Angulo-Brown F, Paez-Hernandez RT. First-order irreversible thermodynamic approach to a simple energy converter. Phys Rev E Stat Nonlin Soft Matter Phys. 2008 Jan;77(1):011123. doi: 10.1103/PhysRevE.77.011123. Epub 2008 Jan 28. PMID: 18351834.
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Subcellular localization of fructosyl amino acid oxidases in peroxisomes of Aspergillus terreus and Penicillium janthinellum.

Journal of bioscience and bioengineering

Sakai Y, Yoshida H, Yurimoto H, Takabe K, Kato N.
PMID: 16232435
J Biosci Bioeng. 1999;87(1):108-11. doi: 10.1016/s1389-1723(99)80018-8.

Fructosyl amino acid oxidase (FAOD) is the enzyme catalyzing the oxidative deglycation of Amadori compounds, such as fructosyl amino acids, yielding the corresponding amino acids, glucosone, and H(2)O(2). In a previous report, we determined the primary structures of cDNAs...

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Sakai Y, Yoshida H, Yurimoto H, et al. Subcellular localization of fructosyl amino acid oxidases in peroxisomes of Aspergillus terreus and Penicillium janthinellum. J Biosci Bioeng. 1999;87(1):108-11doi: 10.1016/s1389-1723(99)80018-8.
Sakai, Y., Yoshida, H., Yurimoto, H., Takabe, K., & Kato, N. (1999). Subcellular localization of fructosyl amino acid oxidases in peroxisomes of Aspergillus terreus and Penicillium janthinellum. Journal of bioscience and bioengineering, 87(1), 108-11. https://doi.org/10.1016/s1389-1723(99)80018-8
Sakai, Y, et al. "Subcellular localization of fructosyl amino acid oxidases in peroxisomes of Aspergillus terreus and Penicillium janthinellum." Journal of bioscience and bioengineering vol. 87,1 (1999): 108-11. doi: https://doi.org/10.1016/s1389-1723(99)80018-8
Sakai Y, Yoshida H, Yurimoto H, Takabe K, Kato N. Subcellular localization of fructosyl amino acid oxidases in peroxisomes of Aspergillus terreus and Penicillium janthinellum. J Biosci Bioeng. 1999;87(1):108-11. doi: 10.1016/s1389-1723(99)80018-8. PMID: 16232435.
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Purification and Characterization of an Enantioselective Amidase from Pseudomonas chlororaphis B23.

Applied and environmental microbiology

Ciskanik LM, Wilczek JM, Fallon RD.
PMID: 16534982
Appl Environ Microbiol. 1995 Mar;61(3):998-1003. doi: 10.1128/aem.61.3.998-1003.1995.

An amidase produced by Pseudomonas chlororaphis B23 was purified and characterized. The purification procedure used included ammonium sulfate precipitation and hydrophobic, anion-exchange, gel filtration, and ceramic hydroxyapatite chromatography steps. This amidase has a native molecular mass of about 105...

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Ciskanik LM, Wilczek JM, Fallon RD. Purification and Characterization of an Enantioselective Amidase from Pseudomonas chlororaphis B23. Appl Environ Microbiol. 1995;61(3):998-1003doi: 10.1128/aem.61.3.998-1003.1995.
Ciskanik, L. M., Wilczek, J. M., & Fallon, R. D. (1995). Purification and Characterization of an Enantioselective Amidase from Pseudomonas chlororaphis B23. Applied and environmental microbiology, 61(3), 998-1003. https://doi.org/10.1128/aem.61.3.998-1003.1995
Ciskanik, L M, et al. "Purification and Characterization of an Enantioselective Amidase from Pseudomonas chlororaphis B23." Applied and environmental microbiology vol. 61,3 (1995): 998-1003. doi: https://doi.org/10.1128/aem.61.3.998-1003.1995
Ciskanik LM, Wilczek JM, Fallon RD. Purification and Characterization of an Enantioselective Amidase from Pseudomonas chlororaphis B23. Appl Environ Microbiol. 1995 Mar;61(3):998-1003. doi: 10.1128/aem.61.3.998-1003.1995. PMID: 16534982; PMCID: PMC1388381.
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Immunogold localization of acyl carrier protein in plants and Escherichia coli: Evidence for membrane association in plants.

Planta

Slabas AR, Smith CG.
PMID: 24221708
Planta. 1988 Aug;175(2):145-52. doi: 10.1007/BF00392423.

Immunogold labelling was used to study the distribution of acyl carrier protein (ACP) in Escherichia coli and a variety of plant tissues. In E. coli, ACP is distributed throughout the cytoplasm, confirming the observation of S. Jackowski et al....

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Slabas AR, Smith CG. Immunogold localization of acyl carrier protein in plants and Escherichia coli: Evidence for membrane association in plants. Planta. 1988;175(2):145-52doi: 10.1007/BF00392423.
Slabas, A. R., & Smith, C. G. (1988). Immunogold localization of acyl carrier protein in plants and Escherichia coli: Evidence for membrane association in plants. Planta, 175(2), 145-52. https://doi.org/10.1007/BF00392423
Slabas, A R, and Smith, C G. "Immunogold localization of acyl carrier protein in plants and Escherichia coli: Evidence for membrane association in plants." Planta vol. 175,2 (1988): 145-52. doi: https://doi.org/10.1007/BF00392423
Slabas AR, Smith CG. Immunogold localization of acyl carrier protein in plants and Escherichia coli: Evidence for membrane association in plants. Planta. 1988 Aug;175(2):145-52. doi: 10.1007/BF00392423. PMID: 24221708.
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Adenylate effects on protein phosphorylation in the interenvelope lumen of pea chloroplasts.

Planta

Soll J, Berger V, Bennett J.
PMID: 24212433
Planta. 1989 Mar;177(3):393-400. doi: 10.1007/BF00403598.

A 64-kilodalton (kDa) protein, situated in the lumen between the inner and outer envelopes of pea (Pisum sativum L.) chloroplasts (Soll and Bennett 1988, Eur. J. Biochem., 175, 301-307) is shown to undergo reversible phosphorylation in isolated mixed envelope...

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Soll J, Berger V, Bennett J. Adenylate effects on protein phosphorylation in the interenvelope lumen of pea chloroplasts. Planta. 1989;177(3):393-400doi: 10.1007/BF00403598.
Soll, J., Berger, V., & Bennett, J. (1989). Adenylate effects on protein phosphorylation in the interenvelope lumen of pea chloroplasts. Planta, 177(3), 393-400. https://doi.org/10.1007/BF00403598
Soll, J, et al. "Adenylate effects on protein phosphorylation in the interenvelope lumen of pea chloroplasts." Planta vol. 177,3 (1989): 393-400. doi: https://doi.org/10.1007/BF00403598
Soll J, Berger V, Bennett J. Adenylate effects on protein phosphorylation in the interenvelope lumen of pea chloroplasts. Planta. 1989 Mar;177(3):393-400. doi: 10.1007/BF00403598. PMID: 24212433.
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Showing 1 to 12 of 67 entries