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Expression of cytochrome P450 enzymes in the cervix. An immunohistochemical study.

International journal of gynecological cancer : official journal of the International Gynecological Cancer Society

Patel KR, Astley S, Adams DJ, Lacey CJ, Ali SW, Wells M.
PMID: 11578337
Int J Gynecol Cancer. 1993 May;3(3):159-163. doi: 10.1046/j.1525-1438.1993.03030159.x.

The expression of cytochrome P450 isoenzymes (subfamilies) CYP1A, CYP2B, CYP2C, CYP3A and CYP4A in the histologically normal cervix was explored using a panel of polyclonal antibodies. There was variation in the intensity of immunohistochemical reaction between the isoenzymes and...

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Patel KR, Astley S, Adams DJ, et al. Expression of cytochrome P450 enzymes in the cervix. An immunohistochemical study. Int J Gynecol Cancer. 1993;3(3):159-163doi: 10.1046/j.1525-1438.1993.03030159.x.
Patel, K. R., Astley, S., Adams, D. J., Lacey, C. J., Ali, S. W., & Wells, M. (1993). Expression of cytochrome P450 enzymes in the cervix. An immunohistochemical study. International journal of gynecological cancer : official journal of the International Gynecological Cancer Society, 3(3), 159-163. https://doi.org/10.1046/j.1525-1438.1993.03030159.x
Patel, K.R., et al. "Expression of cytochrome P450 enzymes in the cervix. An immunohistochemical study." International journal of gynecological cancer : official journal of the International Gynecological Cancer Society vol. 3,3 (1993): 159-163. doi: https://doi.org/10.1046/j.1525-1438.1993.03030159.x
Patel KR, Astley S, Adams DJ, Lacey CJ, Ali SW, Wells M. Expression of cytochrome P450 enzymes in the cervix. An immunohistochemical study. Int J Gynecol Cancer. 1993 May;3(3):159-163. doi: 10.1046/j.1525-1438.1993.03030159.x. PMID: 11578337.
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Cloning and Sequencing of Genes Encoding Phospholipase A(2) from Agkistrodon acutus.

Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica

Liu XL, Pan H, Yang GZ, Wu XF, Zhou YC.
PMID: 12142913
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 1999;31(1):41-45.

Synthetic oligonucleotides were used to amplify phospholipase A(2) (PLA(2)) gene by RT-PCR from total RNA of snake Agkistrodon acutus venom gland. The PCR products were subcloned and positive clones were screened with acidic PLA(2) gene from Agkistrodon halys Pallas....

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Liu XL, Pan H, Yang GZ, et al. Cloning and Sequencing of Genes Encoding Phospholipase A(2) from Agkistrodon acutus. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 1999;31(1):41-45
Liu, X. L., Pan, H., Yang, G. Z., Wu, X. F., & Zhou, Y. C. (1999). Cloning and Sequencing of Genes Encoding Phospholipase A(2) from Agkistrodon acutus. Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica, 31(1), 41-45.
Liu, Xiao-Long, et al. "Cloning and Sequencing of Genes Encoding Phospholipase A(2) from Agkistrodon acutus." Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica vol. 31,1 (1999): 41-45.
Liu XL, Pan H, Yang GZ, Wu XF, Zhou YC. Cloning and Sequencing of Genes Encoding Phospholipase A(2) from Agkistrodon acutus. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 1999;31(1):41-45. PMID: 12142913.
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An Inducible Glutathione S-Transferase in Soybean Hypocotyl Is Localized in the Apoplast.

Plant physiology

Flury T, Wagner E, Kreuz K.
PMID: 12226439
Plant Physiol. 1996 Nov;112(3):1185-1190. doi: 10.1104/pp.112.3.1185.

Glutathione S-transferases (GSTs) with additional activities as fatty acid hydroperoxidases were investigated in soybean (Glycine max L.) hypocotyls. Aside from the GSTs present in total soluble tissue extracts, enzyme activities and distinct immunoreactive GST polypeptides were also detected in...

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Flury T, Wagner E, Kreuz K. An Inducible Glutathione S-Transferase in Soybean Hypocotyl Is Localized in the Apoplast. Plant Physiol. 1996;112(3):1185-1190doi: 10.1104/pp.112.3.1185.
Flury, T., Wagner, E., & Kreuz, K. (1996). An Inducible Glutathione S-Transferase in Soybean Hypocotyl Is Localized in the Apoplast. Plant physiology, 112(3), 1185-1190. https://doi.org/10.1104/pp.112.3.1185
Flury, T., et al. "An Inducible Glutathione S-Transferase in Soybean Hypocotyl Is Localized in the Apoplast." Plant physiology vol. 112,3 (1996): 1185-1190. doi: https://doi.org/10.1104/pp.112.3.1185
Flury T, Wagner E, Kreuz K. An Inducible Glutathione S-Transferase in Soybean Hypocotyl Is Localized in the Apoplast. Plant Physiol. 1996 Nov;112(3):1185-1190. doi: 10.1104/pp.112.3.1185. PMID: 12226439; PMCID: PMC158045.
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Immunopurification and Immunocharacterization of the Glucosinolate Biosynthetic Enzyme Thiohydroximate S-Glucosyltransferase.

Plant physiology

GrootWassink J, Reed DW, Kolenovsky AD.
PMID: 12232212
Plant Physiol. 1994 May;105(1):425-433. doi: 10.1104/pp.105.1.425.

Preparing homogeneous UDP-glucose:thiohydroximate S-glucosyltransferase (S-GT), the penultimate biosynthetic enzyme of glucosinolates, by standard chromatographic methods has yielded too little protein for adequate purity evaluation, identity verification, and structural analysis. The low yields were apparently due to low abundance in...

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GrootWassink J, Reed DW, Kolenovsky AD. Immunopurification and Immunocharacterization of the Glucosinolate Biosynthetic Enzyme Thiohydroximate S-Glucosyltransferase. Plant Physiol. 1994;105(1):425-433doi: 10.1104/pp.105.1.425.
GrootWassink, J., Reed, D. W., & Kolenovsky, A. D. (1994). Immunopurification and Immunocharacterization of the Glucosinolate Biosynthetic Enzyme Thiohydroximate S-Glucosyltransferase. Plant physiology, 105(1), 425-433. https://doi.org/10.1104/pp.105.1.425
GrootWassink, JWD., et al. "Immunopurification and Immunocharacterization of the Glucosinolate Biosynthetic Enzyme Thiohydroximate S-Glucosyltransferase." Plant physiology vol. 105,1 (1994): 425-433. doi: https://doi.org/10.1104/pp.105.1.425
GrootWassink J, Reed DW, Kolenovsky AD. Immunopurification and Immunocharacterization of the Glucosinolate Biosynthetic Enzyme Thiohydroximate S-Glucosyltransferase. Plant Physiol. 1994 May;105(1):425-433. doi: 10.1104/pp.105.1.425. PMID: 12232212; PMCID: PMC159371.
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Comparative Studies on Ferredoxin-NADP+ Oxidoreductase Isoenzymes Derived from Different Organs by Antibodies Specific for the Radish Root- and Leaf-Enzymes.

Plant physiology

Morigasaki S, Jin T, Wada K.
PMID: 12231952
Plant Physiol. 1993 Oct;103(2):435-440. doi: 10.1104/pp.103.2.435.

Determination of the prosthetic group and titration of sulfhydryl group of ferredoxin-NADP+ oxidoreductase (FNR) from roots of radish (Raphanus sativus var acanthiformis cv Miyashige) confirmed its similarity to leaf-FNR. Antisera directed against radish root-FNR and leaf-FNR distinguished the enzyme...

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Morigasaki S, Jin T, Wada K. Comparative Studies on Ferredoxin-NADP+ Oxidoreductase Isoenzymes Derived from Different Organs by Antibodies Specific for the Radish Root- and Leaf-Enzymes. Plant Physiol. 1993;103(2):435-440doi: 10.1104/pp.103.2.435.
Morigasaki, S., Jin, T., & Wada, K. (1993). Comparative Studies on Ferredoxin-NADP+ Oxidoreductase Isoenzymes Derived from Different Organs by Antibodies Specific for the Radish Root- and Leaf-Enzymes. Plant physiology, 103(2), 435-440. https://doi.org/10.1104/pp.103.2.435
Morigasaki, S., et al. "Comparative Studies on Ferredoxin-NADP+ Oxidoreductase Isoenzymes Derived from Different Organs by Antibodies Specific for the Radish Root- and Leaf-Enzymes." Plant physiology vol. 103,2 (1993): 435-440. doi: https://doi.org/10.1104/pp.103.2.435
Morigasaki S, Jin T, Wada K. Comparative Studies on Ferredoxin-NADP+ Oxidoreductase Isoenzymes Derived from Different Organs by Antibodies Specific for the Radish Root- and Leaf-Enzymes. Plant Physiol. 1993 Oct;103(2):435-440. doi: 10.1104/pp.103.2.435. PMID: 12231952; PMCID: PMC159001.
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Effects of Elevated Cytosolic Glutathione Reductase Activity on the Cellular Glutathione Pool and Photosynthesis in Leaves under Normal and Stress Conditions.

Plant physiology

Foyer C, Lelandais M, Galap C, Kunert KJ.
PMID: 16668524
Plant Physiol. 1991 Nov;97(3):863-72. doi: 10.1104/pp.97.3.863.

Tobacco (Nicotiana tabacum var Samsun) was transformed using the bacterial gor gene coding for the enzyme glutathione reductase. Transgenic plants were selected by their kanamycin resistence and expression of the bacterial gor gene. After separation by isoelectric focusing techniques,...

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Foyer C, Lelandais M, Galap C, et al. Effects of Elevated Cytosolic Glutathione Reductase Activity on the Cellular Glutathione Pool and Photosynthesis in Leaves under Normal and Stress Conditions. Plant Physiol. 1991;97(3):863-72doi: 10.1104/pp.97.3.863.
Foyer, C., Lelandais, M., Galap, C., & Kunert, K. J. (1991). Effects of Elevated Cytosolic Glutathione Reductase Activity on the Cellular Glutathione Pool and Photosynthesis in Leaves under Normal and Stress Conditions. Plant physiology, 97(3), 863-72. https://doi.org/10.1104/pp.97.3.863
Foyer, C, et al. "Effects of Elevated Cytosolic Glutathione Reductase Activity on the Cellular Glutathione Pool and Photosynthesis in Leaves under Normal and Stress Conditions." Plant physiology vol. 97,3 (1991): 863-72. doi: https://doi.org/10.1104/pp.97.3.863
Foyer C, Lelandais M, Galap C, Kunert KJ. Effects of Elevated Cytosolic Glutathione Reductase Activity on the Cellular Glutathione Pool and Photosynthesis in Leaves under Normal and Stress Conditions. Plant Physiol. 1991 Nov;97(3):863-72. doi: 10.1104/pp.97.3.863. PMID: 16668524; PMCID: PMC1081097.
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The cloning, genetic mapping, and expression of the constitutive sucrose synthase locus of maize.

Proceedings of the National Academy of Sciences of the United States of America

McCarty DR, Shaw JR, Hannah LC.
PMID: 16593784
Proc Natl Acad Sci U S A. 1986 Dec;83(23):9099-103. doi: 10.1073/pnas.83.23.9099.

Two differentially expressed genes encode isoenzymes of sucrose synthase in Zea mays. A clone of the shrunken 1 (Sh1) locus, the structural gene for the major endosperm form of sucrose synthase, was used to isolate a genomic clone of...

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McCarty DR, Shaw JR, Hannah LC. The cloning, genetic mapping, and expression of the constitutive sucrose synthase locus of maize. Proc Natl Acad Sci U S A. 1986;83(23):9099-103doi: 10.1073/pnas.83.23.9099.
McCarty, D. R., Shaw, J. R., & Hannah, L. C. (1986). The cloning, genetic mapping, and expression of the constitutive sucrose synthase locus of maize. Proceedings of the National Academy of Sciences of the United States of America, 83(23), 9099-103. https://doi.org/10.1073/pnas.83.23.9099
McCarty, D R, et al. "The cloning, genetic mapping, and expression of the constitutive sucrose synthase locus of maize." Proceedings of the National Academy of Sciences of the United States of America vol. 83,23 (1986): 9099-103. doi: https://doi.org/10.1073/pnas.83.23.9099
McCarty DR, Shaw JR, Hannah LC. The cloning, genetic mapping, and expression of the constitutive sucrose synthase locus of maize. Proc Natl Acad Sci U S A. 1986 Dec;83(23):9099-103. doi: 10.1073/pnas.83.23.9099. PMID: 16593784; PMCID: PMC387082.
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Specific peroxidase isoenzymes are correlated with organogenesis.

Plant physiology

Kay LE, Basile DV.
PMID: 16665414
Plant Physiol. 1987 May;84(1):99-105. doi: 10.1104/pp.84.1.99.

We have examined isoperoxidase patterns obtained from buffer-, salt-, and enzyme-extractable fractions and correlated them with histological changes in tobacco (Nicotiana tabacum L., cv Wisc. 38) ;epidermal' explants induced to produce either callus, vegetative buds, or floral buds. By...

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Kay LE, Basile DV. Specific peroxidase isoenzymes are correlated with organogenesis. Plant Physiol. 1987;84(1):99-105doi: 10.1104/pp.84.1.99.
Kay, L. E., & Basile, D. V. (1987). Specific peroxidase isoenzymes are correlated with organogenesis. Plant physiology, 84(1), 99-105. https://doi.org/10.1104/pp.84.1.99
Kay, L E, and Basile, D V. "Specific peroxidase isoenzymes are correlated with organogenesis." Plant physiology vol. 84,1 (1987): 99-105. doi: https://doi.org/10.1104/pp.84.1.99
Kay LE, Basile DV. Specific peroxidase isoenzymes are correlated with organogenesis. Plant Physiol. 1987 May;84(1):99-105. doi: 10.1104/pp.84.1.99. PMID: 16665414; PMCID: PMC1056535.
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Isolation and characterization of the cytosolic and chloroplastic 3-phosphoglycerate kinase from spinach leaves.

Plant physiology

Köpke-Secundo E, Molnar I, Schnarrenberger C.
PMID: 16667463
Plant Physiol. 1990 May;93(1):40-7. doi: 10.1104/pp.93.1.40.

The cytosol and chloroplast 3-phosphoglycerate kinases (3-PGK) from spinach (Spinacia oleracea L.) were purifled to apparent homogeneity. The procedure included a conventional anion-exchange chromatography on DEAE-cellulose and mainly a series of HPLC columns. The charge differences of the two...

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Köpke-Secundo E, Molnar I, Schnarrenberger C. Isolation and characterization of the cytosolic and chloroplastic 3-phosphoglycerate kinase from spinach leaves. Plant Physiol. 1990;93(1):40-7doi: 10.1104/pp.93.1.40.
Köpke-Secundo, E., Molnar, I., & Schnarrenberger, C. (1990). Isolation and characterization of the cytosolic and chloroplastic 3-phosphoglycerate kinase from spinach leaves. Plant physiology, 93(1), 40-7. https://doi.org/10.1104/pp.93.1.40
Köpke-Secundo, E, et al. "Isolation and characterization of the cytosolic and chloroplastic 3-phosphoglycerate kinase from spinach leaves." Plant physiology vol. 93,1 (1990): 40-7. doi: https://doi.org/10.1104/pp.93.1.40
Köpke-Secundo E, Molnar I, Schnarrenberger C. Isolation and characterization of the cytosolic and chloroplastic 3-phosphoglycerate kinase from spinach leaves. Plant Physiol. 1990 May;93(1):40-7. doi: 10.1104/pp.93.1.40. PMID: 16667463; PMCID: PMC1062464.
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High resolution of peroxidase-indoleacetic Acid oxidase isoenzymes from horseradish by isoelectric focusing.

Plant physiology

Hoyle MC.
PMID: 16660185
Plant Physiol. 1977 Nov;60(5):787-93. doi: 10.1104/pp.60.5.787.

Several improved techniques for isoelectric focusing of isoenzymes in polyacrylamide gel slabs were developed. Using these techniques, three commercial sources of horseradish peroxidase were each examined with three commercial sources of carrier ampholytes to determine their respective isoenzyme profiles.A...

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Hoyle MC. High resolution of peroxidase-indoleacetic Acid oxidase isoenzymes from horseradish by isoelectric focusing. Plant Physiol. 1977;60(5):787-93doi: 10.1104/pp.60.5.787.
Hoyle, M. C. (1977). High resolution of peroxidase-indoleacetic Acid oxidase isoenzymes from horseradish by isoelectric focusing. Plant physiology, 60(5), 787-93. https://doi.org/10.1104/pp.60.5.787
Hoyle, M C. "High resolution of peroxidase-indoleacetic Acid oxidase isoenzymes from horseradish by isoelectric focusing." Plant physiology vol. 60,5 (1977): 787-93. doi: https://doi.org/10.1104/pp.60.5.787
Hoyle MC. High resolution of peroxidase-indoleacetic Acid oxidase isoenzymes from horseradish by isoelectric focusing. Plant Physiol. 1977 Nov;60(5):787-93. doi: 10.1104/pp.60.5.787. PMID: 16660185; PMCID: PMC542715.
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Development of (1-->3,1-->4)-beta-d-Glucan Endohydrolase Isoenzymes in Isolated Scutella and Aleurone Layers of Barley (Hordeum vulgare).

Plant physiology

Stuart IM, Loi L, Fincher GB.
PMID: 16664619
Plant Physiol. 1986 Feb;80(2):310-4. doi: 10.1104/pp.80.2.310.

An immunological assay has been used to investigate the synthesis of (1-->3,1-->4)-beta-glucanase (EC 3.2.1.73) isoenzymes from isolated barley aleurone layers and scutella. Enzyme release from both tissues is enhanced by 1 micromolar gibberellic acid and 10 millimolar Ca(2+), although...

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Stuart IM, Loi L, Fincher GB. Development of (1-->3,1-->4)-beta-d-Glucan Endohydrolase Isoenzymes in Isolated Scutella and Aleurone Layers of Barley (Hordeum vulgare). Plant Physiol. 1986;80(2):310-4doi: 10.1104/pp.80.2.310.
Stuart, I. M., Loi, L., & Fincher, G. B. (1986). Development of (1-->3,1-->4)-beta-d-Glucan Endohydrolase Isoenzymes in Isolated Scutella and Aleurone Layers of Barley (Hordeum vulgare). Plant physiology, 80(2), 310-4. https://doi.org/10.1104/pp.80.2.310
Stuart, I M, et al. "Development of (1-->3,1-->4)-beta-d-Glucan Endohydrolase Isoenzymes in Isolated Scutella and Aleurone Layers of Barley (Hordeum vulgare)." Plant physiology vol. 80,2 (1986): 310-4. doi: https://doi.org/10.1104/pp.80.2.310
Stuart IM, Loi L, Fincher GB. Development of (1-->3,1-->4)-beta-d-Glucan Endohydrolase Isoenzymes in Isolated Scutella and Aleurone Layers of Barley (Hordeum vulgare). Plant Physiol. 1986 Feb;80(2):310-4. doi: 10.1104/pp.80.2.310. PMID: 16664619; PMCID: PMC1075110.
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Regulation of Aspartate Kinase Isoenzymes in Barley Mutants Resistant to Lysine plus Threonine : Construction and Analysis of Combinations of the Lt1a, Lt1b, and Lt2 Mutant Genes.

Plant physiology

Arruda P, Bright SW, Kueh JS, Lea PJ, Rognes SE.
PMID: 16663861
Plant Physiol. 1984 Oct;76(2):442-6. doi: 10.1104/pp.76.2.442.

Two homozygous mutant lines of barley (Hordeum vulgare L.) R3202 (Lt1b/Lt1b) and R3004 (Lt2/Lt2), are resistant to lysine plus threonine. They contain aspartate kinase isoenzymes with lost or decreased feedback sensitivity to lysine in either isoenzyme AKII (R3202) or...

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Arruda P, Bright SW, Kueh JS, et al. Regulation of Aspartate Kinase Isoenzymes in Barley Mutants Resistant to Lysine plus Threonine : Construction and Analysis of Combinations of the Lt1a, Lt1b, and Lt2 Mutant Genes. Plant Physiol. 1984;76(2):442-6doi: 10.1104/pp.76.2.442.
Arruda, P., Bright, S. W., Kueh, J. S., Lea, P. J., & Rognes, S. E. (1984). Regulation of Aspartate Kinase Isoenzymes in Barley Mutants Resistant to Lysine plus Threonine : Construction and Analysis of Combinations of the Lt1a, Lt1b, and Lt2 Mutant Genes. Plant physiology, 76(2), 442-6. https://doi.org/10.1104/pp.76.2.442
Arruda, P, et al. "Regulation of Aspartate Kinase Isoenzymes in Barley Mutants Resistant to Lysine plus Threonine : Construction and Analysis of Combinations of the Lt1a, Lt1b, and Lt2 Mutant Genes." Plant physiology vol. 76,2 (1984): 442-6. doi: https://doi.org/10.1104/pp.76.2.442
Arruda P, Bright SW, Kueh JS, Lea PJ, Rognes SE. Regulation of Aspartate Kinase Isoenzymes in Barley Mutants Resistant to Lysine plus Threonine : Construction and Analysis of Combinations of the Lt1a, Lt1b, and Lt2 Mutant Genes. Plant Physiol. 1984 Oct;76(2):442-6. doi: 10.1104/pp.76.2.442. PMID: 16663861; PMCID: PMC1064307.
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Showing 25 to 36 of 740 entries