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  • Inorganic mercury  (1)
  • Liver  (1)
  • Protein binding  (1)
  • 1
    ISSN: 1432-0738
    Keywords: Methylmercury ; Protein synthesis ; Liver ; Adrenal ; Rat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract (1) A single injection of methylmercury chloride in the rat (10–50 mg/kg) increased both in vivo and in vitro rates of 14C-leucine incorporation into the protein of the post-mitochondrial supernatant fraction of the liver. In contrast, no stimulation of protein synthesis was observed in the brain of the methylmercury-treated rats. (2) Methylmercury administration also stimulated RNA polymerase activities in isolated hepatic nuclei, stimulation of Mg-dependent activity being higher than that of Mn-dependent activity. (3) In experiments with adrenalectomized rats, it was found that the stimulatory effect of methylmercury on protein and RNA synthesis in the liver was mediated partly through the adrenal gland. (4) Analysis of serum by starch-block electrophoresis revealed that synthesis of all serum proteins, including albumin and α-γ globulin fractions, was stimulated by methylmercury treatment. (5) These results suggest that the observed effects of methylmercury on the liver depend on mechanisms other than enhancement of the synthesis of acute-phase proteins.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0738
    Keywords: Methylmercury ; Protein binding ; Peripheral nerves ; Myelin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A small amount of a glycoprotein species (21-kDa glycoprotein) with high affinity for methylmercury (MeHg) was detected in the post-nuclear or post-mitochondrial supernatant fraction of the homogenate of rat sciatic nerve on electrophoresis and autoradiography after binding of Me203Hg to the fraction. The 21-kDa glycoprotein was also found in the subcellular fractions of mouse, hamster, guinea pig, rabbit and human peripheral nervous tissues. Experiments with the cellular fractions of the tissues revealed that the 21-kDa glycoprotein is localized mainly in the myelin fraction, whereas it was not found in the cellular fractions of brain, spinal cord and nonneural tissues, such as kidney and liver. The specific binding activity of the 21-kDa glycoprotein with MeHg was 12–15 fold that of the major myelin protein, Po. It was shown that the interaction of the 21-kDa glycoprotein with MeHg was mediated through sulfhydryl groups in experiments with iodoacetamide and dithiothreitol. The amino acid compositions of the rat and human 21-kDa glycoproteins were similar but very different from that of a typical metallothionein. The N-terminal amino acid sequences of the two components of the rat 21-kDa glycoprotein were identical to those of Po and PMP-22, respectively. The in vitro binding of MeHg was also observed in the myelin fraction obtained from the sciatic nerves of MeHg-dosed rats.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0738
    Keywords: Methylmercury ; Inorganic mercury ; Rat ; Subcellular distribution ; Biotransformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Accumulation of inorganic mercury in subcellular fractions of the kidney, liver, and brain of rats was studied during 48 days after a single injection of 25 mg/kg of methylmercury chloride. The highest ratio of inorganic to total mercury was seen in the cytosol of kidney, 80% of the total being as inorganic mercury at day 48. The ratio in the mitochondria and microsomes of kidney attained a maximum level (about 50% of the total as inorganic) at day 26–37. In the liver, the ratio was strikingly low in the cytosol and microsomes as compared to the light and heavy mitochondria where about 40% of the total was present as inorganic maximally at day 26. The ratio in the brain, determined up to day 15, was very low as compared with the kidney and liver, showing less than 3% of the total in the mitochondria, microsomes, and cytosol, and 5.4% in the myelin fraction. The high accumulation of inorganic mercury in the cytosol of kidney was closely related to metallothionein-like component, while those in the mitochondria and microsomes of kidney and in the mitochondria of liver were exclusively bound to high molecular weight proteins even after deoxycholate treatment.
    Type of Medium: Electronic Resource
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