JUAN BAUTISTA
BARROSO ALBARRACÍN
CATEDRATICO DE UNIVERSIDAD
José Antonio
Lupiáñez Cara
Publicaciones en las que colabora con José Antonio Lupiáñez Cara (21)
2008
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Serine dehydratase and tyrosine aminotransferase activities increased by long-term starvation and recovery by refeeding in rainbow trout (Oncorhynchus mykiss)
Journal of Experimental Zoology Part A: Ecological Genetics and Physiology, Vol. 309, Núm. 1, pp. 25-34
2006
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Downregulation in the expression of the serine dehydratase in the rat liver during chronic metabolic acidosis
American Journal of Physiology - Regulatory Integrative and Comparative Physiology, Vol. 291, Núm. 5
2005
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Serine dehydratase expression decreases in rat livers injured by chronic thioacetamide ingestion
Molecular and Cellular Biochemistry, Vol. 268, Núm. 1-2, pp. 33-43
2001
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Carbohydrate deprivation reduces NADPH-production in fish liver but not in adipose tissue
International Journal of Biochemistry and Cell Biology, Vol. 33, Núm. 8, pp. 785-796
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Growth, protein-turnover rates and nucleic-acid concentrations in the white muscle of rainbow trout during development
International Journal of Biochemistry and Cell Biology, Vol. 33, Núm. 12, pp. 1227-1238
2000
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Dietary alterations in protein, carbohydrates and fat increase liver protein-turnover rate and decrease overall growth rate in the rainbow trout (Oncorhynchus mykiss)
Molecular and Cellular Biochemistry, Vol. 209, Núm. 1-2, pp. 97-104
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Molecular and kinetic characterization and cell type location of inducible nitric oxide synthase in fish
American Journal of Physiology - Regulatory Integrative and Comparative Physiology, Vol. 279, Núm. 2 48-2
1999
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Carbohydrates affect protein-turnover rates, growth, and nucleic acid content in the white muscle of rainbow trout (Oncorhynchus mykiss)
Aquaculture, Vol. 179, Núm. 1-4, pp. 425-437
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Kinetic behavior and protein expression of hepatic NADPH-production systems during development of rainbow trout (Oncorhynchus mykiss)
Aquaculture, Vol. 179, Núm. 1-4, pp. 375-385
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Localization of nitric-oxide synthase in plant peroxisomes
Journal of Biological Chemistry, Vol. 274, Núm. 51, pp. 36729-36733
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Peroxisomal NADP-dependent isocitrate dehydrogenase. Characterization and activity regulation during natural senescence
Plant Physiology, Vol. 121, Núm. 3, pp. 921-928
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Selective changes in the protein-turnover rates and nature of growth induced in trout liver by long-term starvation followed by re-feeding
Molecular and Cellular Biochemistry, Vol. 201, Núm. 1-2, pp. 1-10
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Variations in the kinetic behaviour of the NADPH-production systems in different tissues of the trout when fed on an amino-acid-based diet at different frequencies
International Journal of Biochemistry and Cell Biology, Vol. 31, Núm. 2, pp. 277-290
1998
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A dehydrogenase-mediated recycling system of NADPH in plant peroxisomes
Biochemical Journal, Vol. 330, Núm. 2, pp. 777-784
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Impact of starvation-refeeding on kinetics and protein expression of trout liver NADPH-production systems
American Journal of Physiology - Regulatory Integrative and Comparative Physiology, Vol. 274, Núm. 6 43-6
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Relationship between growth and protein turnover rates and nucleic acids in the liver of rainbow trout (Oncorhynchus mykiss) during development
Canadian Journal of Fisheries and Aquatic Sciences, Vol. 55, Núm. 3, pp. 649-657
1995
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Kinetic properties of hexose-monophosphate dehydrogenases. II. Isolation and partial purification of 6-phosphogluconate dehydrogenase from rat liver and kidney cortex
Molecular and Cellular Biochemistry, Vol. 144, Núm. 2, pp. 97-104
1994
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Dietary protein effects on growth and fractional protein synthesis and degradation rates in liver and white muscle of rainbow trout (Oncorhynchus mykiss)
Aquaculture, Vol. 124, Núm. 1-4, pp. 35-46
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The influence of dietary protein on the kinetics of NADPH production systems in various tissues of rainbow trout (Oncorhynchus mykiss)
Aquaculture, Vol. 124, Núm. 1-4, pp. 47-59
1992
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Alterations in the fractional protein turnover rates in rainbow-trout liver and white muscle caused by an aminoacid-based diet and changes in the feeding frequency
Toxicological & Environmental Chemistry, Vol. 36, Núm. 3-4, pp. 217-224