The uptake and K(+)-evoked (40 mM) release of 3H-norepinephrine (3H-NE) in mesodiencephalic synaptosomes of adult and senescent rats and the effect of N-acetylaspartic acid (NAA) on these processes have been studied. It has been shown that the uptake of 3H-NE by old rats is reduced considerably. The K(+)-evoked release of 3H-NE from rats synaptosomes is significantly decreased in aged rats.
View Article and Find Full Text PDFIt was demonstrated that the NADPH-adrenodoxin reductase molecule contains ten tryptophan residues titrated by N-bromosuccinimide. The effectiveness of the non-radiant energy transfer was used to calculate the average distance between the NADPH-binding site of the enzyme and tryptophan residues at different steps of N-bromosuccinimide-induced modification.
View Article and Find Full Text PDFZh Evol Biokhim Fiziol
January 1987
Serotonin content of the epiphysis has been studied in 1-day chicks, 1-, 5-5 1/2-, 8-12- and 24-month hens. It was found that this content undergoes significant changes during life cycle of hens, being dependent on physiological activity of the gonads. The highest level of serotonin (16 micrograms/g) was observed in 8-12 months old hens which corresponds to the period of the most intensive activity of the gonads.
View Article and Find Full Text PDFSynaptosomal fractions were isolated from rat cerebral cortex immediately after decapitation and after 2 h and 4 h postmortem storage at room temperature. Uptake and release of [3H]GABA was compared between fresh and postmortem synaptosomal fractions. The results suggest that after a 2 h postmortem storage these functions are still comparable to those observed in fresh preparations, while a 4 h period of storage decreases them by about 50%.
View Article and Find Full Text PDFThe fluorescent and phosphorescent properties of NADPH-adrenodoxin reductase were investigated. It was shown that the fluorescence of protein tryptophanyls was quenched completely by acrylamide and partially by ionic quenchers (I- and Cs+). A removal of the prosthetic group from the protein causes insignificant changes in fluorescent properties of the enzyme.
View Article and Find Full Text PDF