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    1. The effects of acetaminophen on human liver proteins and their activities have not been investigated, finally. The use of human liver tissue, liver slices, and hepatocytes, and functional proteomics approaches should yield substantial new information in all of these areas. Hepatocyte plasma membrane Na /K -ATPase activity is also significantly inhibited after hepatoxic doses of acetaminophen in rats (216), and despite attempts to detect adducts, none have been detected to this ATPase (160). It is known that hepatotoxic doses of acetaminophen affect some hepatocyte enzyme activities early in the pathogenesis of toxicity without detectable adduct formation, additionally.

    “Noncovalent” Interactions with Cellular Proteins As evident from Table 2, there are some hepatic proteins whose basal levels are decreased after acetaminophen administration to mice, yet no protein adducts have been identified. Several other enzymes, and a few receptor and structural proteins, form covalent adducts with reactive metabolites of acetaminophen (Table 4) but it is not yet known if their activities or functions are affected. For example, there is evidence that acetaminophen, through its reactive metabolite NAPQI, inhibits calcium-dependent ATPases (204,146,201–215), but no adducts to these ATPases have been identified. Furthermore, the time courses of adduct formation, repair, and/or degradation, and of activity and function are unknown for most of the proteins identified (see below).

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    Hepatitis B virus brand viagra 100mg price. N Engl J Med. 1977;354(13):832-7.

    Dynamics and impact of perinatal transmission of hepatitis B virus in North India.

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    Inhibition of hepatocytary vesicular transport by cyclosporin A in the rat. Transplantation 1985.

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