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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European journal of clinical pharmacology 37 (1989), S. 501-506 
    ISSN: 1432-1041
    Keywords: N-acetylcysteine ; paracetamol ; acetaminophen overdose ; pharmacokinetics ; liver damage ; adverse reactions ; dose modifications
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary Seventeen patients received standard treatment with intravenous N-acetylcysteine for 18 episodes of severe poisoning with paracetamol (acetaminophen). The dose of N-acetylcysteine was 150 mg/kg given in 15 min followed by 50 mg/kg in 4 h and 100 mg/kg over the next 16 h. Liver damage was absent or mild on 13 occasions (ALT〈500 µ/l) and severe on 5 (ALT〉1000 µ/l). Total plasma N-acetylcysteine was estimated by HPLC. The mean maximum plasma concentration after the initial loading dose was 554 mg/l. Concentrations then fell rapidly and after 12 h a mean steady-state level of about 35 mg/l was maintained. When the infusion was discontinued N-acetylcysteine disappeared with a half-life of 5.7 h. The mean steady-state volume of distribution, AUC, mean residence time and total clearance were 536 ml/kg, 1748 mg·h·l−1, 2.91 h and 3.18 ml·min−1·kg−1. These values are generally consistent with those previously reported with much smaller doses and the disposition of N-acetylcysteine does not appear to be dose-dependent. The elimination of N-acetylcysteine was not impaired in the patients with severe liver damage, and the pharmacokinetic variables and plasma concentrations were similar in patients with and without hepatotoxicity. The dosage schedule for intravenous N-acetylcysteine should probably be modified since adverse reactions invariably occur early when plasma concentrations are at their highest, and liver damage was prevented just as effectively at the lowest as at the highest Cmax. High initial concentrations of N-acetylcysteine can be avoided with simple alternative regimens based on the kinetic data of this study.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: SUMMARY– A longer whip time is usually required to obtain a meringue of the same specific gravity from pasteurized egg white as from unpasteurized egg white. We have determined the rate at which this change in whipping properties occurs as a function of heating time and pH. The rate of damage is minimal at neutral pH. The activation energy for whipping property damage at pH 7.5 is 140 kcal. Experiments in which either ovomucin or lysozyme concentration of egg white was increased and decreased showed that the reaction producing damage to the whipping properties is first order with respect to both ovomucin and lysozyme concentration. Since an increase of 0.33 in the ionic strength of egg white produces a ten-fold decrease in the rate of whipping property damage, the reactants are probably present as the ovomucin-lysozyme electrostatic complex. The product appears to be an irreversibly denatured ovomucin-lysozyme aggregate or network. Removal of the product restores the whipping properties of the egg white. The whipping property damage is a decrease in the mechanical stability of the foam. For this reason a longer time is needed to whip pasteurized egg white to a satisfactory meringue. Whipping aids such as triethyl citrate or triethyl phosphate compensate for the damage to the whipping properties, but do not appear to reverse the reaction producing damage to the whipping properties of the egg white.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: SUMMARY– Enzymatic activity of β-N-acetylglucosaminidase, which occurs naturally in chicken egg white, was characterized to establish conditions suitable for routine assay for this enzyme in egg products. A variation in enzyme content of approximately 3-fold was observed in individual fresh eggs. The enzyme has a pH optimum between 3.0 and 3.4, and a Km of approximately 0.6 mM for the substrate p-nitrophenyl-N-acetyl-β-D-glucosaminide. Activation energy for hydrolysis of this substrate is 10.7±0.8 kcal/mole. The enzyme is stable for at least several hours at ambient temperature from pH 6.8 to approximately 8.8. Above pH 8.8, inactivation is first order with respect to time. Enzyme activity in shell eggs decreases fairly rapidly at ambient temperature; loss of activity probably results from increase in pH of egg white, which occurs normally upon loss of carbon dioxide. Eggs held at 4°C retain activity much longer.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    BJOG 77 (1970), S. 0 
    ISSN: 1471-0528
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Of a total of 576 patients with cervical carcinoma in situ, 75 have shown evidence of persistent disease after various initial treatments. None of the 75 have developed invasive cervical cancer during follow-up.This result is used to obtain confidence limits for the probability with which carcinoma in situ will become invasive and for the period after which it does so. Two separate assumptions about the distribution of latent periods give comparable values for these limits, which imply a low invasive potential in conservatively treated carcinoma in situ.With the further assumption that the treatments used have not altered the course of the disease, the need for any treatment at all and the effectiveness of cervical cytology screening programmes are questioned.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 36 (1971), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: SUMMARY– The kinetics of the heat inactivation of β-N-acetylglucosaminidase in egg white and whole egg at neutral pH is first order in the temperature range 58–62°C. Rate constants for enzyme inactivation by heat are reported for both egg white and whole egg. The activation energy for heat denaturation is 91 kcal/mole in egg white and 73 kcal/mole in whole egg. Reduction of enzymatic activity upon heating can be used as an indication of whether egg white or whole egg has been maintained at the time-temperature combinations approved for pasteurization by the U.S. Department of Agriculture. This test should be useful as a process control tool.
    Type of Medium: Electronic Resource
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