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Showing 1 to 12 of 25 entries
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Staurosporine-induced apoptosis of immortalized mouse proximal tubule cells is modulated by bcl-2 expression level.

Biochemistry and molecular biology international

Takeda M, Kobayashi M, Osaki T, Shirato I, Endou H.
PMID: 19856280
Biochem Mol Biol Int. 1997 Jul;42(4):649-56. doi: 10.1080/15216549700203061.

Mouse terminal proximal tubule (S3)cells treated with staurosporine (STS) underwent morphological and biochemical changes characteristic of apoptosis. Treatment of S3 cells with STS, H-7, PMA, herbimycin A or genistein caused DNA fragmentation. STS inhibited the activity of protein kinase...

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Takeda M, Kobayashi M, Osaki T, et al. Staurosporine-induced apoptosis of immortalized mouse proximal tubule cells is modulated by bcl-2 expression level. Biochem Mol Biol Int. 1997;42(4):649-56doi: 10.1080/15216549700203061.
Takeda, M., Kobayashi, M., Osaki, T., Shirato, I., & Endou, H. (1997). Staurosporine-induced apoptosis of immortalized mouse proximal tubule cells is modulated by bcl-2 expression level. Biochemistry and molecular biology international, 42(4), 649-56. https://doi.org/10.1080/15216549700203061
Takeda, M, et al. "Staurosporine-induced apoptosis of immortalized mouse proximal tubule cells is modulated by bcl-2 expression level." Biochemistry and molecular biology international vol. 42,4 (1997): 649-56. doi: https://doi.org/10.1080/15216549700203061
Takeda M, Kobayashi M, Osaki T, Shirato I, Endou H. Staurosporine-induced apoptosis of immortalized mouse proximal tubule cells is modulated by bcl-2 expression level. Biochem Mol Biol Int. 1997 Jul;42(4):649-56. doi: 10.1080/15216549700203061. PMID: 19856280.
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Effect of dihydralazine on the fluidity of erythrocyte membranes.

Biochemistry and molecular biology international

Maliszewska-Mazur M, Sikorski AF, Jezierski A.
PMID: 19856285
Biochem Mol Biol Int. 1997 Jul;42(4):693-9. doi: 10.1080/15216549700203111.

Dihydralazine, a drug used in the treatment of chronic hypertension was found to affect the mobility of fatty acid hydrocarbon chains followed by spin-labelling technique with the use of 5-, 12- and 16-doxylstearate. The effect of this drug on...

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Maliszewska-Mazur M, Sikorski AF, Jezierski A. Effect of dihydralazine on the fluidity of erythrocyte membranes. Biochem Mol Biol Int. 1997;42(4):693-9doi: 10.1080/15216549700203111.
Maliszewska-Mazur, M., Sikorski, A. F., & Jezierski, A. (1997). Effect of dihydralazine on the fluidity of erythrocyte membranes. Biochemistry and molecular biology international, 42(4), 693-9. https://doi.org/10.1080/15216549700203111
Maliszewska-Mazur, M, et al. "Effect of dihydralazine on the fluidity of erythrocyte membranes." Biochemistry and molecular biology international vol. 42,4 (1997): 693-9. doi: https://doi.org/10.1080/15216549700203111
Maliszewska-Mazur M, Sikorski AF, Jezierski A. Effect of dihydralazine on the fluidity of erythrocyte membranes. Biochem Mol Biol Int. 1997 Jul;42(4):693-9. doi: 10.1080/15216549700203111. PMID: 19856285.
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The histidine-805 in motif-C of the phage SP6 RNA polymerase is essential for its activity as revealed by random mutagenesis.

Biochemistry and molecular biology international

Jeong W, Kang C.
PMID: 19856287
Biochem Mol Biol Int. 1997 Jul;42(4):711-6. doi: 10.1080/15216549700203131.

In order to identify functional residues of the bacteriophage SP6 RNA polymerase, its C-terminal one-twelfth region was randomly mutagenized using polymerase chain reactions of its gene under the conditions for reduced fidelity of Taq DNA polymerase. Using a two-vector...

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Jeong W, Kang C. The histidine-805 in motif-C of the phage SP6 RNA polymerase is essential for its activity as revealed by random mutagenesis. Biochem Mol Biol Int. 1997;42(4):711-6doi: 10.1080/15216549700203131.
Jeong, W., & Kang, C. (1997). The histidine-805 in motif-C of the phage SP6 RNA polymerase is essential for its activity as revealed by random mutagenesis. Biochemistry and molecular biology international, 42(4), 711-6. https://doi.org/10.1080/15216549700203131
Jeong, W, and Kang, C. "The histidine-805 in motif-C of the phage SP6 RNA polymerase is essential for its activity as revealed by random mutagenesis." Biochemistry and molecular biology international vol. 42,4 (1997): 711-6. doi: https://doi.org/10.1080/15216549700203131
Jeong W, Kang C. The histidine-805 in motif-C of the phage SP6 RNA polymerase is essential for its activity as revealed by random mutagenesis. Biochem Mol Biol Int. 1997 Jul;42(4):711-6. doi: 10.1080/15216549700203131. PMID: 19856287.
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The priming effects of some human interleukins on the production of leukotrienes by calcium ionophore stimulated leukocytes.

Biochemistry and molecular biology international

Mansour M, El-Ahmady O, Motawi T.
PMID: 19856299
Biochem Mol Biol Int. 1997 Jul;42(4):817-24. doi: 10.1080/15216549700203251.

This study demonstrates the changing levels of leukotrieneB4 (LTB4) and leukotrieneC4 (LTC4) generated by human white blood cells primed with different human interleukins IL-3, IL-5, IL-6, IL-8 and with human hematopoietic growth factor granulocyte-macrophage colony stimulating factor (GM-CSF). Preincubation...

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Mansour M, El-Ahmady O, Motawi T. The priming effects of some human interleukins on the production of leukotrienes by calcium ionophore stimulated leukocytes. Biochem Mol Biol Int. 1997;42(4):817-24doi: 10.1080/15216549700203251.
Mansour, M., El-Ahmady, O., & Motawi, T. (1997). The priming effects of some human interleukins on the production of leukotrienes by calcium ionophore stimulated leukocytes. Biochemistry and molecular biology international, 42(4), 817-24. https://doi.org/10.1080/15216549700203251
Mansour, M, et al. "The priming effects of some human interleukins on the production of leukotrienes by calcium ionophore stimulated leukocytes." Biochemistry and molecular biology international vol. 42,4 (1997): 817-24. doi: https://doi.org/10.1080/15216549700203251
Mansour M, El-Ahmady O, Motawi T. The priming effects of some human interleukins on the production of leukotrienes by calcium ionophore stimulated leukocytes. Biochem Mol Biol Int. 1997 Jul;42(4):817-24. doi: 10.1080/15216549700203251. PMID: 19856299.
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Efficient production of active TNF-alpha by albumin signal peptide.

Biochemistry and molecular biology international

Maeda Y, Soda M, Ito K, Sato K.
PMID: 19856300
Biochem Mol Biol Int. 1997 Jul;42(4):825-32. doi: 10.1080/15216549700203261.

TNF-alpha is initially synthesized as a membrane-anchored precursor protein and processed proteolytically by a matrix metalloproteinase (MMP)-like enzyme. In order to establish an efficient expression system of TNF-alpha in mammalian cells without involvement of the extracellular enzyme, an expression...

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Maeda Y, Soda M, Ito K, et al. Efficient production of active TNF-alpha by albumin signal peptide. Biochem Mol Biol Int. 1997;42(4):825-32doi: 10.1080/15216549700203261.
Maeda, Y., Soda, M., Ito, K., & Sato, K. (1997). Efficient production of active TNF-alpha by albumin signal peptide. Biochemistry and molecular biology international, 42(4), 825-32. https://doi.org/10.1080/15216549700203261
Maeda, Y, et al. "Efficient production of active TNF-alpha by albumin signal peptide." Biochemistry and molecular biology international vol. 42,4 (1997): 825-32. doi: https://doi.org/10.1080/15216549700203261
Maeda Y, Soda M, Ito K, Sato K. Efficient production of active TNF-alpha by albumin signal peptide. Biochem Mol Biol Int. 1997 Jul;42(4):825-32. doi: 10.1080/15216549700203261. PMID: 19856300.
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Expression or possession of catalase gene does not alter the capacity of M. smegmatis to survive within human macrophages.

Biochemistry and molecular biology international

Fazal N.
PMID: 19856302
Biochem Mol Biol Int. 1997 Jul;42(4):843-51. doi: 10.1080/15216549700203281.

Mycobacterium tuberculosis genes are expressed and screened in Mycobacterium smegmatis as a host, hence their survival in human monocytes needs to be determined. Strains of Mycobacterium smegmatis with an inactive catalase-peroxidase gene (KatG), or into which the KatG gene...

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Fazal N. Expression or possession of catalase gene does not alter the capacity of M. smegmatis to survive within human macrophages. Biochem Mol Biol Int. 1997;42(4):843-51doi: 10.1080/15216549700203281.
Fazal, N. (1997). Expression or possession of catalase gene does not alter the capacity of M. smegmatis to survive within human macrophages. Biochemistry and molecular biology international, 42(4), 843-51. https://doi.org/10.1080/15216549700203281
Fazal, N. "Expression or possession of catalase gene does not alter the capacity of M. smegmatis to survive within human macrophages." Biochemistry and molecular biology international vol. 42,4 (1997): 843-51. doi: https://doi.org/10.1080/15216549700203281
Fazal N. Expression or possession of catalase gene does not alter the capacity of M. smegmatis to survive within human macrophages. Biochem Mol Biol Int. 1997 Jul;42(4):843-51. doi: 10.1080/15216549700203281. PMID: 19856302.
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Cytotoxic activity of acetylcholine receptor ligands.

Biochemistry and molecular biology international

Blishchenko EY, Mirkina II, Mernenko OA, Yatskin ON, Satpaev DK, Strizhkov BN, Karelin AA.
PMID: 19856291
Biochem Mol Biol Int. 1997 Jul;42(4):739-47. doi: 10.1080/15216549700203171.

Acetylcholine receptor ligands were studied for cytotoxicity in K562 human erythroid leukemia tumor cells. Cytotoxicity of carbachol, an agonist of acetylcholine receptors, atropine, an antagonist of muscarinic acetylcholine receptor, neurotoxin 11 (NT II) from Naja naja oxiana cobra venom...

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Blishchenko EY, Mirkina II, Mernenko OA, et al. Cytotoxic activity of acetylcholine receptor ligands. Biochem Mol Biol Int. 1997;42(4):739-47doi: 10.1080/15216549700203171.
Blishchenko, E. Y., Mirkina, I. I., Mernenko, O. A., Yatskin, O. N., Satpaev, D. K., Strizhkov, B. N., & Karelin, A. A. (1997). Cytotoxic activity of acetylcholine receptor ligands. Biochemistry and molecular biology international, 42(4), 739-47. https://doi.org/10.1080/15216549700203171
Blishchenko, E Y, et al. "Cytotoxic activity of acetylcholine receptor ligands." Biochemistry and molecular biology international vol. 42,4 (1997): 739-47. doi: https://doi.org/10.1080/15216549700203171
Blishchenko EY, Mirkina II, Mernenko OA, Yatskin ON, Satpaev DK, Strizhkov BN, Karelin AA. Cytotoxic activity of acetylcholine receptor ligands. Biochem Mol Biol Int. 1997 Jul;42(4):739-47. doi: 10.1080/15216549700203171. PMID: 19856291.
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Protoporphyrin IX potentiates horseradish peroxidase-catalyzed oxidation of NADH:Involvement of enzyme-porphyrin interaction.

Biochemistry and molecular biology international

Sil S, Chakraborti AS.
PMID: 19856293
Biochem Mol Biol Int. 1997 Jul;42(4):759-68. doi: 10.1080/15216549700203191.

Protoporphyrin IX potentiates horseradish peroxidase-catalyzed hydrogen peroxide-mediated NADH oxidation, but the porphyrin cannot change the enzyme-catalyzed o-dianisidine oxidation. Spectrofluorimetric studies reveal that an interaction occurs between horseradish peroxidase and protoporphyrin IX. The interaction is predominantly hydrophobic and entropy-driven endothermic...

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Sil S, Chakraborti AS. Protoporphyrin IX potentiates horseradish peroxidase-catalyzed oxidation of NADH:Involvement of enzyme-porphyrin interaction. Biochem Mol Biol Int. 1997;42(4):759-68doi: 10.1080/15216549700203191.
Sil, S., & Chakraborti, A. S. (1997). Protoporphyrin IX potentiates horseradish peroxidase-catalyzed oxidation of NADH:Involvement of enzyme-porphyrin interaction. Biochemistry and molecular biology international, 42(4), 759-68. https://doi.org/10.1080/15216549700203191
Sil, S, and Chakraborti, A S. "Protoporphyrin IX potentiates horseradish peroxidase-catalyzed oxidation of NADH:Involvement of enzyme-porphyrin interaction." Biochemistry and molecular biology international vol. 42,4 (1997): 759-68. doi: https://doi.org/10.1080/15216549700203191
Sil S, Chakraborti AS. Protoporphyrin IX potentiates horseradish peroxidase-catalyzed oxidation of NADH:Involvement of enzyme-porphyrin interaction. Biochem Mol Biol Int. 1997 Jul;42(4):759-68. doi: 10.1080/15216549700203191. PMID: 19856293.
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The activity of branched-chain alpha-keto acid dehydrogenase complex in rat digestive tracts: Effects of dietary protein and exercise.

Biochemistry and molecular biology international

Tsukamura M, Goto H, Arisawa T, Hayakawa T, Kobayashi R, Nakai N, Murakami T, Sugiyama S, Shimomura Y.
PMID: 19856288
Biochem Mol Biol Int. 1997 Jul;42(4):717-22. doi: 10.1080/15216549700203141.

Branched-chain alpha-keto acid dehydrogenase complex is the rate limiting enzyme in catabolism of branched-chain amino acids. In this study, we examined effects of dietary protein and exercise on the complex activity in digestive tracts (stomach, small intestine and colon)...

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Tsukamura M, Goto H, Arisawa T, et al. The activity of branched-chain alpha-keto acid dehydrogenase complex in rat digestive tracts: Effects of dietary protein and exercise. Biochem Mol Biol Int. 1997;42(4):717-22doi: 10.1080/15216549700203141.
Tsukamura, M., Goto, H., Arisawa, T., Hayakawa, T., Kobayashi, R., Nakai, N., Murakami, T., Sugiyama, S., & Shimomura, Y. (1997). The activity of branched-chain alpha-keto acid dehydrogenase complex in rat digestive tracts: Effects of dietary protein and exercise. Biochemistry and molecular biology international, 42(4), 717-22. https://doi.org/10.1080/15216549700203141
Tsukamura, M, et al. "The activity of branched-chain alpha-keto acid dehydrogenase complex in rat digestive tracts: Effects of dietary protein and exercise." Biochemistry and molecular biology international vol. 42,4 (1997): 717-22. doi: https://doi.org/10.1080/15216549700203141
Tsukamura M, Goto H, Arisawa T, Hayakawa T, Kobayashi R, Nakai N, Murakami T, Sugiyama S, Shimomura Y. The activity of branched-chain alpha-keto acid dehydrogenase complex in rat digestive tracts: Effects of dietary protein and exercise. Biochem Mol Biol Int. 1997 Jul;42(4):717-22. doi: 10.1080/15216549700203141. PMID: 19856288.
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Production and characterisation of monoclonal and polyclonal amtobpdoes agaomst bovine osteocalcin.

Biochemistry and molecular biology international

Nielsen PK, Hønberg LS, Larsen T, Sperling-Petersena HU, Sottrup-Jensen L.
PMID: 19856292
Biochem Mol Biol Int. 1997 Jul;42(4):749-57. doi: 10.1080/15216549700203181.

Monoclonal and polyclonal antibodies were produced against osteocalcin purified from bovine bone. The antibodies were used for the development of a two-site ELISA. A monoclonal antibody recognising residues 15-49 of bovine osteocatcin generated by cleavage with 70% formic acid...

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Nielsen PK, Hønberg LS, Larsen T, et al. Production and characterisation of monoclonal and polyclonal amtobpdoes agaomst bovine osteocalcin. Biochem Mol Biol Int. 1997;42(4):749-57doi: 10.1080/15216549700203181.
Nielsen, P. K., Hønberg, L. S., Larsen, T., Sperling-Petersena, H. U., & Sottrup-Jensen, L. (1997). Production and characterisation of monoclonal and polyclonal amtobpdoes agaomst bovine osteocalcin. Biochemistry and molecular biology international, 42(4), 749-57. https://doi.org/10.1080/15216549700203181
Nielsen, P K, et al. "Production and characterisation of monoclonal and polyclonal amtobpdoes agaomst bovine osteocalcin." Biochemistry and molecular biology international vol. 42,4 (1997): 749-57. doi: https://doi.org/10.1080/15216549700203181
Nielsen PK, Hønberg LS, Larsen T, Sperling-Petersena HU, Sottrup-Jensen L. Production and characterisation of monoclonal and polyclonal amtobpdoes agaomst bovine osteocalcin. Biochem Mol Biol Int. 1997 Jul;42(4):749-57. doi: 10.1080/15216549700203181. PMID: 19856292.
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The structural analysis of the O-glycans of the jacalin-bound rabbit immunoglobulin G.

Biochemistry and molecular biology international

Kabir S, Gerwig GJ.
PMID: 19856294
Biochem Mol Biol Int. 1997 Jul;42(4):769-78. doi: 10.1080/15216549700203201.

Rabbit immunoglobulin G (IgG) is a sialoglycoprotein (2.4% carbohydrate), containing both N-glycolyl (Neu5Gc) and N-acetyl (Neu5Ac) neuraminic acids in a ratio of 87:13. A small fraction of rabbit IgG (about 25% of total IgG) bound to jacalin as demonstrated...

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Kabir S, Gerwig GJ. The structural analysis of the O-glycans of the jacalin-bound rabbit immunoglobulin G. Biochem Mol Biol Int. 1997;42(4):769-78doi: 10.1080/15216549700203201.
Kabir, S., & Gerwig, G. J. (1997). The structural analysis of the O-glycans of the jacalin-bound rabbit immunoglobulin G. Biochemistry and molecular biology international, 42(4), 769-78. https://doi.org/10.1080/15216549700203201
Kabir, S, and Gerwig, G J. "The structural analysis of the O-glycans of the jacalin-bound rabbit immunoglobulin G." Biochemistry and molecular biology international vol. 42,4 (1997): 769-78. doi: https://doi.org/10.1080/15216549700203201
Kabir S, Gerwig GJ. The structural analysis of the O-glycans of the jacalin-bound rabbit immunoglobulin G. Biochem Mol Biol Int. 1997 Jul;42(4):769-78. doi: 10.1080/15216549700203201. PMID: 19856294.
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Reversible cell cycle arrest with concomitant p21/WAF1 overexpression and mitochondrial destruction by nitric oxide.

Biochemistry and molecular biology international

Esumi H, Chin K, Kurashima Y, Hasegawa F, Ogura T, Yoneda M, Ozawa T.
PMID: 19856295
Biochem Mol Biol Int. 1997 Jul;42(4):779-87. doi: 10.1080/15216549700203211.

When human hepatocellular carcinoma Hep-G2 cells were treated with the NO-generating compounds, S-nitroso-N-acetyl-DL-penicillamine(SNAP) or (+/-)-(E)-4-ethyl-2-(E)-hydroxyimino]-5-nitroso-3-hexenamide, cells stopped growing. Most cells were found to be in either G1 or G2/M phase and the dye-exclusion test revealed that the cells were...

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Esumi H, Chin K, Kurashima Y, et al. Reversible cell cycle arrest with concomitant p21/WAF1 overexpression and mitochondrial destruction by nitric oxide. Biochem Mol Biol Int. 1997;42(4):779-87doi: 10.1080/15216549700203211.
Esumi, H., Chin, K., Kurashima, Y., Hasegawa, F., Ogura, T., Yoneda, M., & Ozawa, T. (1997). Reversible cell cycle arrest with concomitant p21/WAF1 overexpression and mitochondrial destruction by nitric oxide. Biochemistry and molecular biology international, 42(4), 779-87. https://doi.org/10.1080/15216549700203211
Esumi, H, et al. "Reversible cell cycle arrest with concomitant p21/WAF1 overexpression and mitochondrial destruction by nitric oxide." Biochemistry and molecular biology international vol. 42,4 (1997): 779-87. doi: https://doi.org/10.1080/15216549700203211
Esumi H, Chin K, Kurashima Y, Hasegawa F, Ogura T, Yoneda M, Ozawa T. Reversible cell cycle arrest with concomitant p21/WAF1 overexpression and mitochondrial destruction by nitric oxide. Biochem Mol Biol Int. 1997 Jul;42(4):779-87. doi: 10.1080/15216549700203211. PMID: 19856295.
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Showing 1 to 12 of 25 entries