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Showing 13 to 24 of 25 entries
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Study of peptide-protein interaction by high-performance liquid chromatography. Effect of hydrophobic and steric parameters.

Biochemistry and molecular biology international

Szikszay Z, Forgács E.
PMID: 19856283
Biochem Mol Biol Int. 1997 Jul;42(4):677-84. doi: 10.1080/15216549700203091.

The interaction of 16 peptides was studied on zein-coated silica column by high-performance liquid chromatography. The separation factor, theoretical plate number and the asymmetry factors of the peaks were calculated. Stepwise regression analysis was applied to study the peptide-protein...

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Szikszay Z, Forgács E. Study of peptide-protein interaction by high-performance liquid chromatography. Effect of hydrophobic and steric parameters. Biochem Mol Biol Int. 1997;42(4):677-84doi: 10.1080/15216549700203091.
Szikszay, Z., & Forgács, E. (1997). Study of peptide-protein interaction by high-performance liquid chromatography. Effect of hydrophobic and steric parameters. Biochemistry and molecular biology international, 42(4), 677-84. https://doi.org/10.1080/15216549700203091
Szikszay, Z, and Forgács, E. "Study of peptide-protein interaction by high-performance liquid chromatography. Effect of hydrophobic and steric parameters." Biochemistry and molecular biology international vol. 42,4 (1997): 677-84. doi: https://doi.org/10.1080/15216549700203091
Szikszay Z, Forgács E. Study of peptide-protein interaction by high-performance liquid chromatography. Effect of hydrophobic and steric parameters. Biochem Mol Biol Int. 1997 Jul;42(4):677-84. doi: 10.1080/15216549700203091. PMID: 19856283.
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Studies on the catalytic activity of human hepatic porphobilinogen deaminase.

Biochemistry and molecular biology international

Mazzetti MB, Tomio JM.
PMID: 19856284
Biochem Mol Biol Int. 1997 Jul;42(4):685-92. doi: 10.1080/15216549700203101.

Porphobilinogen deaminase was purified from human hepatocytes. A variety of group specific reagents have been used to achieve site-specific modifications to evaluate the potential role of such groups in the whole catalytic cycle. Treatment with dicarbonyl reagents caused a...

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Mazzetti MB, Tomio JM. Studies on the catalytic activity of human hepatic porphobilinogen deaminase. Biochem Mol Biol Int. 1997;42(4):685-92doi: 10.1080/15216549700203101.
Mazzetti, M. B., & Tomio, J. M. (1997). Studies on the catalytic activity of human hepatic porphobilinogen deaminase. Biochemistry and molecular biology international, 42(4), 685-92. https://doi.org/10.1080/15216549700203101
Mazzetti, M B, and Tomio, J M. "Studies on the catalytic activity of human hepatic porphobilinogen deaminase." Biochemistry and molecular biology international vol. 42,4 (1997): 685-92. doi: https://doi.org/10.1080/15216549700203101
Mazzetti MB, Tomio JM. Studies on the catalytic activity of human hepatic porphobilinogen deaminase. Biochem Mol Biol Int. 1997 Jul;42(4):685-92. doi: 10.1080/15216549700203101. PMID: 19856284.
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Interactions between heparinoids and alcohol dehydrogenase.

Biochemistry and molecular biology international

Paulíková H, Valusová E, Antalík M.
PMID: 19856282
Biochem Mol Biol Int. 1997 Jul;42(4):667-76. doi: 10.1080/15216549700203081.

The interaction between polysulfated polysaecharides (low-molecular-weight heparin LMWH, dextran sulfate DS and pentosan sulfate PS) and yeast alcohol dehydrogenase (YADH) was investigated. The fluorescence and UV spectra of YADH after adding the tested polysaccharides have confirmed the interaction between...

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Paulíková H, Valusová E, Antalík M. Interactions between heparinoids and alcohol dehydrogenase. Biochem Mol Biol Int. 1997;42(4):667-76doi: 10.1080/15216549700203081.
Paulíková, H., Valusová, E., & Antalík, M. (1997). Interactions between heparinoids and alcohol dehydrogenase. Biochemistry and molecular biology international, 42(4), 667-76. https://doi.org/10.1080/15216549700203081
Paulíková, H, et al. "Interactions between heparinoids and alcohol dehydrogenase." Biochemistry and molecular biology international vol. 42,4 (1997): 667-76. doi: https://doi.org/10.1080/15216549700203081
Paulíková H, Valusová E, Antalík M. Interactions between heparinoids and alcohol dehydrogenase. Biochem Mol Biol Int. 1997 Jul;42(4):667-76. doi: 10.1080/15216549700203081. PMID: 19856282.
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Age- and Tissue-specific regulation of chicken inorganic pyrophosphatase.

Biochemistry and molecular biology international

Syiem D, Sharma R.
PMID: 19856298
Biochem Mol Biol Int. 1997 Jul;42(4):809-15. doi: 10.1080/15216549700203241.

The activities and hormone regulatory patterns of inorganic pyrophosphatase (PPiase) of male Rhode Island Red (RIR) chickens were studied at two different postnatal ages (5- and 90-day). The endogenous activity level was found to be significantly higher in the...

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Syiem D, Sharma R. Age- and Tissue-specific regulation of chicken inorganic pyrophosphatase. Biochem Mol Biol Int. 1997;42(4):809-15doi: 10.1080/15216549700203241.
Syiem, D., & Sharma, R. (1997). Age- and Tissue-specific regulation of chicken inorganic pyrophosphatase. Biochemistry and molecular biology international, 42(4), 809-15. https://doi.org/10.1080/15216549700203241
Syiem, D, and Sharma, R. "Age- and Tissue-specific regulation of chicken inorganic pyrophosphatase." Biochemistry and molecular biology international vol. 42,4 (1997): 809-15. doi: https://doi.org/10.1080/15216549700203241
Syiem D, Sharma R. Age- and Tissue-specific regulation of chicken inorganic pyrophosphatase. Biochem Mol Biol Int. 1997 Jul;42(4):809-15. doi: 10.1080/15216549700203241. PMID: 19856298.
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Quantification of epididymal retinoic acid-binding protein (ERABP) mRNA in different anatomical regions of the adult rat epididymis.

Biochemistry and molecular biology international

Hall JC, Tubbs CE.
PMID: 19856301
Biochem Mol Biol Int. 1997 Jul;42(4):833-41. doi: 10.1080/15216549700203271.

Epididymal retinoic acid-binding protein (ERABP), an 18.5 Kd androgen-dependent protein, is synthesized and secreted by the rat epididymis. The concentration of ERABP mRNA in different anatomical regions of the rat epididymis was measured using quantitative reverse transcription polymerase chain...

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Hall JC, Tubbs CE. Quantification of epididymal retinoic acid-binding protein (ERABP) mRNA in different anatomical regions of the adult rat epididymis. Biochem Mol Biol Int. 1997;42(4):833-41doi: 10.1080/15216549700203271.
Hall, J. C., & Tubbs, C. E. (1997). Quantification of epididymal retinoic acid-binding protein (ERABP) mRNA in different anatomical regions of the adult rat epididymis. Biochemistry and molecular biology international, 42(4), 833-41. https://doi.org/10.1080/15216549700203271
Hall, J C, and Tubbs, C E. "Quantification of epididymal retinoic acid-binding protein (ERABP) mRNA in different anatomical regions of the adult rat epididymis." Biochemistry and molecular biology international vol. 42,4 (1997): 833-41. doi: https://doi.org/10.1080/15216549700203271
Hall JC, Tubbs CE. Quantification of epididymal retinoic acid-binding protein (ERABP) mRNA in different anatomical regions of the adult rat epididymis. Biochem Mol Biol Int. 1997 Jul;42(4):833-41. doi: 10.1080/15216549700203271. PMID: 19856301.
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Heterogeneous nuclear RNP protein A1-arginine methylation during HCT-48 cell cycle.

Biochemistry and molecular biology international

Park SH, Park GH, Gu H, Hwang WI, Lim IK, Paik WK, Kim S.
PMID: 19856281
Biochem Mol Biol Int. 1997 Jul;42(4):657-66. doi: 10.1080/15216549700203071.

Protein methylase I (protein-arginine N-methyltransferase) was examined in HCT-48 cells, synchronized by serum deprivation and hydroxyurea treatment. The enzyme activity to methylate the added hnRNP protein A1 increased about 2-fold from G0 to S phase, and then decreased during...

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Park SH, Park GH, Gu H, et al. Heterogeneous nuclear RNP protein A1-arginine methylation during HCT-48 cell cycle. Biochem Mol Biol Int. 1997;42(4):657-66doi: 10.1080/15216549700203071.
Park, S. H., Park, G. H., Gu, H., Hwang, W. I., Lim, I. K., Paik, W. K., & Kim, S. (1997). Heterogeneous nuclear RNP protein A1-arginine methylation during HCT-48 cell cycle. Biochemistry and molecular biology international, 42(4), 657-66. https://doi.org/10.1080/15216549700203071
Park, S H, et al. "Heterogeneous nuclear RNP protein A1-arginine methylation during HCT-48 cell cycle." Biochemistry and molecular biology international vol. 42,4 (1997): 657-66. doi: https://doi.org/10.1080/15216549700203071
Park SH, Park GH, Gu H, Hwang WI, Lim IK, Paik WK, Kim S. Heterogeneous nuclear RNP protein A1-arginine methylation during HCT-48 cell cycle. Biochem Mol Biol Int. 1997 Jul;42(4):657-66. doi: 10.1080/15216549700203071. PMID: 19856281.
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Recombinant CTFR detection in CF tracheal epithelial cells following in vitro liposomeme-mediated gene transfer.

Biochemistry and molecular biology international

Colosimo A, Scarpino S, Sangiuolo F, Sario SD, Mossa G, Novelli G, Dallapiccola B.
PMID: 19856289
Biochem Mol Biol Int. 1997 Jul;42(4):723-9. doi: 10.1080/15216549700203151.

The efficacy of CFTR gene transfer mediated by cationic liposomes Dc-Chol/DOPE into cystic fibrosis (CF) tracheal epithelial cells carrying defective processing mutations (S549N/N1303K), was assessed by studying mRNA and protein expression of the recombinant product. Appreciable levels of mRNA...

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Colosimo A, Scarpino S, Sangiuolo F, et al. Recombinant CTFR detection in CF tracheal epithelial cells following in vitro liposomeme-mediated gene transfer. Biochem Mol Biol Int. 1997;42(4):723-9doi: 10.1080/15216549700203151.
Colosimo, A., Scarpino, S., Sangiuolo, F., Sario, S. D., Mossa, G., Novelli, G., & Dallapiccola, B. (1997). Recombinant CTFR detection in CF tracheal epithelial cells following in vitro liposomeme-mediated gene transfer. Biochemistry and molecular biology international, 42(4), 723-9. https://doi.org/10.1080/15216549700203151
Colosimo, A, et al. "Recombinant CTFR detection in CF tracheal epithelial cells following in vitro liposomeme-mediated gene transfer." Biochemistry and molecular biology international vol. 42,4 (1997): 723-9. doi: https://doi.org/10.1080/15216549700203151
Colosimo A, Scarpino S, Sangiuolo F, Sario SD, Mossa G, Novelli G, Dallapiccola B. Recombinant CTFR detection in CF tracheal epithelial cells following in vitro liposomeme-mediated gene transfer. Biochem Mol Biol Int. 1997 Jul;42(4):723-9. doi: 10.1080/15216549700203151. PMID: 19856289.
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A protease from the marine sponge Callyspongia schulzi.

Biochemistry and molecular biology international

Mebs D, Benesch S, König B, Yamakawa Y, Omori-Satoh T.
PMID: 19856296
Biochem Mol Biol Int. 1997 Jul;42(4):789-97. doi: 10.1080/15216549700203221.

Aqueous extracts of 25 marine sponge species (from coral reefs of Papua New Guinea) were screened for proteolytic activity. Only one sponge, Callyspongia schulzi, showed remarkable activity. A protease hydrolyzing casein as well as the synthetic substrate alpha-N-benzoyl-L-arginine ethyl...

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Mebs D, Benesch S, König B, et al. A protease from the marine sponge Callyspongia schulzi. Biochem Mol Biol Int. 1997;42(4):789-97doi: 10.1080/15216549700203221.
Mebs, D., Benesch, S., König, B., Yamakawa, Y., & Omori-Satoh, T. (1997). A protease from the marine sponge Callyspongia schulzi. Biochemistry and molecular biology international, 42(4), 789-97. https://doi.org/10.1080/15216549700203221
Mebs, D, et al. "A protease from the marine sponge Callyspongia schulzi." Biochemistry and molecular biology international vol. 42,4 (1997): 789-97. doi: https://doi.org/10.1080/15216549700203221
Mebs D, Benesch S, König B, Yamakawa Y, Omori-Satoh T. A protease from the marine sponge Callyspongia schulzi. Biochem Mol Biol Int. 1997 Jul;42(4):789-97. doi: 10.1080/15216549700203221. PMID: 19856296.
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Mutational analysis for the role of C-terminal region of ecotin, a dimeric inhibitor of pancreatic serine proteases.

Biochemistry and molecular biology international

Seong IS, Lee CS, Park HK, Suh SW, Kang MS, Chung CH.
PMID: 19856297
Biochem Mol Biol Int. 1997 Jul;42(4):799-807. doi: 10.1080/15216549700203231.

Ecotin is a dimeric molecule that is capable of inhibiting a variety of serine proteases. To clarify the role of the C-terminal region, mutagenesis was performed to delete the C-terminal residues from 130 to 142. The mutant inhibitor behaved...

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Seong IS, Lee CS, Park HK, et al. Mutational analysis for the role of C-terminal region of ecotin, a dimeric inhibitor of pancreatic serine proteases. Biochem Mol Biol Int. 1997;42(4):799-807doi: 10.1080/15216549700203231.
Seong, I. S., Lee, C. S., Park, H. K., Suh, S. W., Kang, M. S., & Chung, C. H. (1997). Mutational analysis for the role of C-terminal region of ecotin, a dimeric inhibitor of pancreatic serine proteases. Biochemistry and molecular biology international, 42(4), 799-807. https://doi.org/10.1080/15216549700203231
Seong, I S, et al. "Mutational analysis for the role of C-terminal region of ecotin, a dimeric inhibitor of pancreatic serine proteases." Biochemistry and molecular biology international vol. 42,4 (1997): 799-807. doi: https://doi.org/10.1080/15216549700203231
Seong IS, Lee CS, Park HK, Suh SW, Kang MS, Chung CH. Mutational analysis for the role of C-terminal region of ecotin, a dimeric inhibitor of pancreatic serine proteases. Biochem Mol Biol Int. 1997 Jul;42(4):799-807. doi: 10.1080/15216549700203231. PMID: 19856297.
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First Report of Papaya leaf curl virus Infecting Papaya Plants in Taiwan.

Plant disease

Chang LS, Lee YS, Su HJ, Hung TH.
PMID: 30812941
Plant Dis. 2003 Feb;87(2):204. doi: 10.1094/PDIS.2003.87.2.204A.

Papaya leaf curl disease was first reported in India in 1939 (1). Caused by begomovirus, Papaya leaf curl virus (PaLCV) (2), this disease was discovered in the papaya orchards of southern Taiwan in 2002. Infected papaya developed symptoms such...

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Chang LS, Lee YS, Su HJ, et al. First Report of Papaya leaf curl virus Infecting Papaya Plants in Taiwan. Plant Dis. 2003;87(2):204doi: 10.1094/PDIS.2003.87.2.204A.
Chang, L. S., Lee, Y. S., Su, H. J., & Hung, T. H. (2003). First Report of Papaya leaf curl virus Infecting Papaya Plants in Taiwan. Plant disease, 87(2), 204. https://doi.org/10.1094/PDIS.2003.87.2.204A
Chang, L-S, et al. "First Report of Papaya leaf curl virus Infecting Papaya Plants in Taiwan." Plant disease vol. 87,2 (2003): 204. doi: https://doi.org/10.1094/PDIS.2003.87.2.204A
Chang LS, Lee YS, Su HJ, Hung TH. First Report of Papaya leaf curl virus Infecting Papaya Plants in Taiwan. Plant Dis. 2003 Feb;87(2):204. doi: 10.1094/PDIS.2003.87.2.204A. PMID: 30812941.
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Inhibition of various isoforms of rat liver glutathione S-transferases by tannic acid and butein.

Biochemistry and molecular biology international

Zhang K, Mack P, Wong KP.
PMID: 19856286
Biochem Mol Biol Int. 1997 Jul;42(4):701-10. doi: 10.1080/15216549700203121.

Glutathione S-transferases (EC.2.5.1.18, GSTs) were purified from rat liver by S-hexylglutathione affinity chromatography and six isoforms, namely C-1, C-2, C-3, C-4, A-2 and A-1, were isolated by CM-cellulose and DEAE-cellulose ion-exchange columns. Tannic acid and butein showed varying degrees...

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Zhang K, Mack P, Wong KP. Inhibition of various isoforms of rat liver glutathione S-transferases by tannic acid and butein. Biochem Mol Biol Int. 1997;42(4):701-10doi: 10.1080/15216549700203121.
Zhang, K., Mack, P., & Wong, K. P. (1997). Inhibition of various isoforms of rat liver glutathione S-transferases by tannic acid and butein. Biochemistry and molecular biology international, 42(4), 701-10. https://doi.org/10.1080/15216549700203121
Zhang, K, et al. "Inhibition of various isoforms of rat liver glutathione S-transferases by tannic acid and butein." Biochemistry and molecular biology international vol. 42,4 (1997): 701-10. doi: https://doi.org/10.1080/15216549700203121
Zhang K, Mack P, Wong KP. Inhibition of various isoforms of rat liver glutathione S-transferases by tannic acid and butein. Biochem Mol Biol Int. 1997 Jul;42(4):701-10. doi: 10.1080/15216549700203121. PMID: 19856286.
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An optical biosensor study of the interaction parameters and role of hydrophobic tails of cytochrome P450 2B4, b5 and NADPH-flavoprotein in complex formation.

Biochemistry and molecular biology international

Ivanov YD, Kanaeva IP, Eldarov MA, Sklyabin KG, Lehnerer M, Schulze J, Hlavica P, Archakov AI.
PMID: 19856290
Biochem Mol Biol Int. 1997 Jul;42(4):731-7. doi: 10.1080/15216549700203161.

The real-time interactions of membrane proteins - cytochrome P450 2B4, NADPH cytochrome P450 reductase and cytochrome b5 - were studied by use of an optical biosensor system. The association and dissociation rate constants for the individual complexes were measured...

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Ivanov YD, Kanaeva IP, Eldarov MA, et al. An optical biosensor study of the interaction parameters and role of hydrophobic tails of cytochrome P450 2B4, b5 and NADPH-flavoprotein in complex formation. Biochem Mol Biol Int. 1997;42(4):731-7doi: 10.1080/15216549700203161.
Ivanov, Y. D., Kanaeva, I. P., Eldarov, M. A., Sklyabin, K. G., Lehnerer, M., Schulze, J., Hlavica, P., & Archakov, A. I. (1997). An optical biosensor study of the interaction parameters and role of hydrophobic tails of cytochrome P450 2B4, b5 and NADPH-flavoprotein in complex formation. Biochemistry and molecular biology international, 42(4), 731-7. https://doi.org/10.1080/15216549700203161
Ivanov, Y D, et al. "An optical biosensor study of the interaction parameters and role of hydrophobic tails of cytochrome P450 2B4, b5 and NADPH-flavoprotein in complex formation." Biochemistry and molecular biology international vol. 42,4 (1997): 731-7. doi: https://doi.org/10.1080/15216549700203161
Ivanov YD, Kanaeva IP, Eldarov MA, Sklyabin KG, Lehnerer M, Schulze J, Hlavica P, Archakov AI. An optical biosensor study of the interaction parameters and role of hydrophobic tails of cytochrome P450 2B4, b5 and NADPH-flavoprotein in complex formation. Biochem Mol Biol Int. 1997 Jul;42(4):731-7. doi: 10.1080/15216549700203161. PMID: 19856290.
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Showing 13 to 24 of 25 entries