Further investigations should be carried on to evaluate the risk of fipronil in humans. The benzodiazepines are drugs of choice during seizures, B1 agonists and steroids may be useful during severe inhalation exposure.
AMP-deaminase from human liver was purified by two-step phosphocellulose chromatography, and SDS-PAG electrophoresis of the most active enzyme fraction eluted has been performed. The largest of the protein fragments revealed had a size (92 kDa) of an apparent full-size enzyme subunit, and reacted positively with antibodies produced against specific human ampd2 gene product. Three-day storage at cold room temperature modified significantly the electrophoretical pattern of the enzyme, evidencing continuous and progressive degradation of its structure. This is a first report evidencing the presence of apparent full-size form of human liver AMP-deaminase in preparation obtained from endogenous source.
We describe a case of a 21-year-old male bodybuilder who overdosed on Parabolan (trenbolone acetate) because of its anabolic activity. The patient, with no previous medical history, experienced pruritus and yellow discoloration of the skin and sclerae. Basic biochemical laboratory examination revealed signs of cholestasis with a serum bilirubin level of up to 65.5 mg/dl. Because supportive medical treatment was ineffective, the patient was treated with the molecular adsorbent recirculating system (MARS). Five MARS cycles lasting from 8 to 12 hours were performed every second day. The procedure was well tolerated by the patient and resulted in a sustained relief of pruritus. At the 2-month follow-up visit the plasma bilirubin level had decreased to 2 mg/dl.
AMP-deaminase (EC 3.5.4.6) is an enzyme of nucleotide breakdown involved in regulation of adenine nucleotide pool in mammalian cells. Reaction catalysed by AMP-deaminase constitutes a rate-limiting step in adenine nucleotide catabolism in liver. In this study kinetic and regulatory properties of AMP-deaminase purified from normal and cirrhotic human liver were investigated. In comparison to AMP-deaminase extracted from the normal human liver, AMP-deaminase extracted from the cirrhotic liver was less sensitive towards substrate analogues, and only a very limited response towards pH and adenylate energy charge changes tested for enzyme isolated from this tissue source had been observed. At physiological pH 7.0, in the absence and in the presence of important allosteric effectors (ATP, ADP, GTP and orthophosphate), AMP-deaminases from the two sources studied manifested different regulatory profiles, with half-saturation constant (S0.5) values being distinctly higher for the enzyme extracted from the pathological organ. In contrast to AMP-deaminase isolated from the normal, healthy liver, where presence of relatively large (68 kDa) protein fragment was also detected, only smaller protein fragments were identified, while SDS-PAG electrophoresis of AMP-deaminase isolated from the cirrhotic liver was performed. The obtained results indicate clearly that advanced proteolytic processes occurring in the cirrhotic liver may affect structural integrity of AMP-deaminase studied, making enzyme less active and less sensitive to regulatory action of important allosteric effectors.
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