GAS CHROMATOGRAPHY OF ADRENALIN, NORADRENALIN AND RELATED AMINES AS THEIR TRIMETHYLSILYL ETHERS.
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In human adipose tissue in vitro, dose-response curves of lipolytic agents in releasing free fatty acids and glycerol into an albumine-containing medium were followed. Norepinephrine and adrenaline produced about 20% of the maximal effect of isoproterenol, isopropylnorsynephrine about 40%, theophylline more than 100%. Found pD2 values were approximately 7.4 for isoproterenol and norepinephrine, approximately 5.9 for isopropylnorsynephrine. Phentolamine (1 times 10-5 M) elevated the maximal norepinephrine effects up to the isoproterenol maxima. Phenoxybenzamine (1 times 10-5 M) had significantly lower potentiating effects. Phenylephrine depressed lipolytic actions of isoproterenol (1 times 10-6 M) showing the same pI2 value 3.0 as well in human as in rat adipose tissue and exerted per se weak lipolytic effects also. It is concluded neither potentiating actions of alpha-blockers nor depressing effects of phenylephrine in human adipose tissue seem related to affecting adrenergic alpha-receptors. The existence of antilipolytic actions of adrenergic alpha-receptors is questioned.
In human adipose tissue in vitro, dose-response curves were followed for different adrenomimetics releasing free fatty acids and glycerol into an albumin-containing medium. Phenylephrine, salbutamol and t-butyl-norsynephrine produced lipolytic actions whose maximum did not exceed 20% of the maximal isoproterenol lipolysis. Phentolamine (1 x 10(-5) M) did not potentiate the effect of any of these drugs. When using salbutamol or t-butyl-norsynephrine for antagonizing isoproterenol actions, typical antagonism was found. The parallel shift of the isoproterenol curves showed pA2 values 5.8 for salbutamol and 5.7 for t-butyl-norsynephrine. Comparison of human and rat adipose tissue reactivity shows identical affinities of the drugs studied in both tissues, but related to isoproterenol, diminished intrinsic activities of salbutamol and t-butyl-norsynephrine in human adipose tissue.
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Octopine is released from crown gall tumors as a nutrient source and a signal molecule for the plant pathogen Agrobacterium tumefaciens. Some or all octopine-inducible genes are regulated by a protein called OccR. Primer extension analysis showed that OccR protein represses the occR gene and both represses and activates the occQ operon, which is divergently transcribed from occR. These promoters initiate transcription 46 bp apart. This regulatory system was reconstituted in vitro using purified OccR protein and Escherichia coli RNA polymerase. OccR binds with high affinity to a single site overlapping these promoters. Octopine shortens the DNAase I footprint of OccR and increases the gel mobility of OccR-DNA complexes by relaxing an OccR-incited DNA bend.
A simple method for screening drugs that influence tracheobronchial secretion has been described. After i.p. application of a phenol red solution, part of the dye is secreted into the tracheal lumen. This basal secretion is increased by both parasympathomimetics and sympathomimetics. In addition, expectorants are also capable of increasing tracheal phenol red output. Therefore this method is suitable for the study of drugs that may be capable of influencing tracheobronchial secretion.
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