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Cascales C, Craciunescu DG, Martín-Sanz P, et al. Effect of rhodium (III) complex on experimental carcinogenesis in the livers of rats treated with thioacetamide. Biol Trace Elem Res. 1986;11(1):65-73doi: 10.1007/BF02795525.
Cascales, C., Craciunescu, D. G., Martín-Sanz, P., & Cascales, M. (1986). Effect of rhodium (III) complex on experimental carcinogenesis in the livers of rats treated with thioacetamide. Biological trace element research, 11(1), 65-73. https://doi.org/10.1007/BF02795525
Cascales, C, et al. "Effect of rhodium (III) complex on experimental carcinogenesis in the livers of rats treated with thioacetamide." Biological trace element research vol. 11,1 (1986): 65-73. doi: https://doi.org/10.1007/BF02795525
Cascales C, Craciunescu DG, Martín-Sanz P, Cascales M. Effect of rhodium (III) complex on experimental carcinogenesis in the livers of rats treated with thioacetamide. Biol Trace Elem Res. 1986 Dec;11(1):65-73. doi: 10.1007/BF02795525. PMID: 24254504.
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Biol Trace Elem Res. 1986 Dec;11(1):65-73. doi: 10.1007/BF02795525.

Effect of rhodium (III) complex on experimental carcinogenesis in the livers of rats treated with thioacetamide.

Biological trace element research

C Cascales, D G Craciunescu, P Martín-Sanz, M Cascales

Affiliations

  1. Instituto de Bioquímica, Centro Mixto (CSIC-UCM), Facultad de Farmacia, Ciudad Universitaria, 28040, Madrid, Spain.

PMID: 24254504 DOI: 10.1007/BF02795525

Abstract

Enzyme activities and protein content were determined in the cytosolic and mitochondrial fractions of liver homogenates obtained from Rh(III) complex-, thioacetamide- and thioacetamide + Rh(III) complex-treated rats.The Rh(III) complex administered to nonthioacetamide-treated rats produced no significant changes either in the enzymatic activities assayed or in the protein concentration.The Rh(III) complex administered to thioacetamide-treated rats produced significant restoration of the following altered values: cytosolic and mitochondrial aspartate aminotransferase, glutamate dehydrogenase, NADP-isocitrate dehydrogenase, and protein concentration. However, a further increase was produced in the activities of glucose-6-phosphate dehydrogenase and malic enzyme. These increases can be interpreted in terms of an enhancement of the NADPH-dependent detoxifying processes and of nucleic acid synthesis and repair.

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