Selectivity in integration sites of adenoviral DNA.
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Biomedical subjects
Publications and source records attributed to R Neumann.
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Rats show an elevated creatine kinase (CK) activity in plasma after a 20-hour exposure to hypoxia. The increase of CK activity is essentially caused by CK-BB activity attaining its maximum at the 3rd day after exposure to hypoxia. The possibility of establishing a potential brain damage by determining CK-BB activity in plasma is discussed.
In comparison with a control group, significantly lower lecithin:cholesterol acyltransferase activities and HDL-cholesterol values were found in the serum of patients undergoing chronic haemodialysis, while apolipoprotein A concentration remained unchanged. Reduced activity of lecithin:cholesterol acyltransferase is an indication of the abnormal cholesterol metabolism in haemodialysed patients and could be, in addition to other factors, an explanation for the high incidence of cardiovascular diseases in this patient group.
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1. Multiple copies of intact adenovirus type 12 (Ad12) DNA are integrated into the DNA of Ad12-transformed hamster and Ad12-induced rat brain tumor cells. Free viral DNA is not present in the Ad12-transformed lines investigated. 2. Only few sites of integration are found in Al2-transformed hamster and Ad12-induced rat brain tumor cells. Integration may have occurred into repetitive cellular sequences at selective sites. These sites may be different in different cell lines, however, none of these sites has been analyzed in sufficient detail. 3. Three lines of Ad12-induced rat brain tumor cells exhibit identical patterns of integration. These lines have been derived from three brain tumors in one animal and may have evolved from the same transformed cell. 4. In Ad12-induced rat brain tumor cells early and late segments of the viral genome are expressed as polysome-associated messenger RNA. 5. In human cells productively infected with adenovirus type 2 (Ad2), a large number of viral genome copies are linked to cellular DNA early postinfection. There are only a few sites of recombination (illegitimate?) which probably lie in repetitive cellular DNA sequences. The functional significance of this frequent recombination is unknown.
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Bovine erythrocyte acetylcholinesterase and human plasma cholinesterase are irreversibly inhibited by diethylmesoxalate hydrate, the inhibition potency being comparable to that of certian insecticidal organophosphates and carbamates. Insect cholinesterases, however, appear to be much less affected by diethylmesoxalate hydrate. The compound was also found to inhibit the hydrolysis of paraoxon by rabbit plasma A-esterase, but in a reversible mode.
The activity of the creatine kinase isoenzyme BB was determined in the serum of 26 healthy adults and 31 children. The isoenzyme BB could be proved as a normal component in the human serum. In the adults examined, an activity of 0.56 +/- 0.16 I.U./l (x +/- S.D.) was determined. The activity of creatine kinase isoenzyme BB in the serum does not depend on sex but is subject, however, to a strong age dependence. Only at an age of more than 18 years, isoenzyme BB activities adjust to those of adults.
EDTA and EGTA, added to the reaction mixture for the activity determination of creatine kinase, stimulate the activity of creatine kinase to various extents by suppressing the inhibitory effect of Ca2+ ions. The activation effect is highest for isoenzyme BB, less for isoenzyme MB, and lowest for isoenzyme MM.
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Lecithin: cholesterol acyltransferase activity has been measured in serum from patients with various liver disorders and positive LP-X tests and from healthy subjects. Statistical analysis indicated that lecithin: cholesterol acyltransferase activity provided no help in the discrimination between the persons of both groups although the mean activities differed significantly.
25 percent of 776 andrologic patients showed C3c-complement and coeruloplasmin--determined by radial immundiffusion--in their ejaculate. No correlation could be found between these globulines and possible bacterial infections of the genital tract.
Inhibition constants of several formamidines, their corresponding formanilides and other representatives of compounds derived from aniline, such as phenylureas, N-phenyl-carbamates and acylanilides, were determined for rat liver monoamine oxidase. The reversability of the inhibition and the lack of correlation between inhibition potencies and toxicities of the compounds tested add to the opinion that MAO inhibition is not a prominent factor in chlordimeform poisoning.
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Case report of a 31 year old male with a 47-XXY-Klinefelter-syndrome which showed a maximum of 4,0 million spermatozoa/ml with a motility of up to 51% in his ejaculate. No rise of spermatozoa counts could be observed after 3x25 mg mesterolone/day over 8 weeks.
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The action of plasma amine oxidase upon beta-Br-ethylamine beta-Cl-ethylamine, beta-OH-phenylethylamine, and beta-Cl-phenylethylamine was examined. Beta-Br-ethylamine is a substrate and irreversible inactivator of the enzyme. The enzyme becomes covalently labeled by the inactivator. Approximately 2 mol of inactivator are incorporated per mol of enzyme (MW 170,000). The reduced enzyme is not inactivated. The enzyme catalyzes the elimination of HCl from beta-Cl-phenylethylamine to produce phenylacetaldehyde. The rate of the elimination reaction is comparable to the normal oxidative reaction. We conclude that the occurrence of this elimination reaction establishes the ability of the enzyme to catalyze proton abstraction from C-1 of the substrate and that proton abstraction occurs during the catalytic oxidation normally catalyzed by plasma amine oxidase. Beta-Cl-ethylamine is only oxidized to corresponding aldehyde. Beta-OH-phenylethylamine is neither oxidized, nor does elimination occur. It is a competitive inhibitor in the oxidation of benzylamine and in the elimination of HCl from beta-Cl-phenylethylamine.