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Non-nucleated red blood cells from rats contain adenyl cyclase, the activity of which is predominantly localized in the reticulocytes. Basal enzyme activities in membrane preparations from reticulocyte-rich blood (pretreatment of rats with acetyl-phenylhydrazide: about 60% reticuloytes) are about 5 times higher than in preparations from reticulocyte-poor(More)
Red cell ghosts from healthy volunteers and from patients suffering from haemopoietic or haemolytic disorders were differentiated with respect to their basal, sodium fluoride- and isoproterenol-stimulated adenyl cyclase activities; it was investigated whether adenyl cyclase activities are correlated with the reticulocyte counts in the respective blood(More)
Die durch Natriumfluorid und Isoproterenol stimulierbare Adenylcyclase-Aktivität in Erythrocyten-Schatten von 30–240 g schweren Ratten ist direkt proportional dem prozentualen Retikulocytengehalt des Blutes. Hinweise darauf, dass die Adenylcyclase-Aktivität kernloser Erythrocyten nahezu ausschliesslich in den Retikulocyten lokalisiert ist, konnten auch an(More)
Catecholamine inactivating enzymes in red blood cells are preferentially localized in the reticulocytes and not in mature erythrocytes: catechol-O-methyltransferase (COMT) activity in erythrocyte ghost preparations from reticulocyte-rich blood of rats pretreated with acetyl-phenylhydrazine was found to be 5 times higher than in ghosts from reticulocyte-poor(More)
In red cell preparations from reticulocyte-poor (untreated animals; ∼2% reticulocytes) and reticulocyte-rich blood (animals pretreated with acetylphenylhydrazide; ∼60% reticulocytes) of rats, cAMP binding sites and cAMP-dependent protein kinase activities were determined. High affinity binding sites for cAMP were present both in membrane and cytoplasmic(More)
1. After irreversible inhibition of monoamine oxidase (MAO) in rats with hydrazine derivatives (3-amino-2-oxazolidinone, furazolidone, benmoxine) and the non-hydrazine pargyline, recovery of enzyme activity occurred at rates which were characteristic for the organ investigated and independent of the chemical structure of the irreversible inhibitor. The(More)
Membranpäparate aus retikulozytenreichem Rattenblut, erzeugt durch Behandlung der Tiere mit Acetyl-Phenylhydrazin, zeigen eine 5–6mal höhere Catechol-O-Methyltransferaseaktivität als retikulozytenarme Präparate aus dem Blut unbehandelter Kontrolltiere. Die Aktivität der zytoplasmatischen COMT in den beiden Erythrozytensuspensionen unterscheiden sich nicht(More)