The Regional Concentrations of S‐Adenosyl‐l‐Methionine, S‐Adenosyl‐l‐Homocysteine, and Adenosine in Rat Brain
- 1 March 1982
- journal article
- research article
- Published by Wiley in Journal of Neurochemistry
- Vol. 38 (3), 810-815
- https://doi.org/10.1111/j.1471-4159.1982.tb08702.x
Abstract
The concentrations of S-adenosyl-l-methionine (SAM), S-adenosyl-l-homocysteine (SAH), and adenosine (Ado) were determined in whole brain and rat brain regions by HPLC. The whole brain contains, respectively, 22 nmol, 1 nmol, and 64 nmol of SAM, SAH, and Ado per g of wet tissue. Their distribution indicated that SAM and SAH levels are highest in brainstem, whereas the Ado level is highest in cortex. With aging the SAM concentrations decrease in whole brain, brainstem, and hypothalamus (–25%) and SAH levels increase by 90% in striatum and by 160% in cerebellum, while Ado levels are increased in all regions by 100–180%.Keywords
This publication has 36 references indexed in Scilit:
- Decreased in vivo protein and phospholipid methylation after in vivo elevation of brain S-adenosyl-homocysteineBiochemical and Biophysical Research Communications, 1981
- In Vitro and In Vivo Binding of S‐Adenosyl‐L‐Homocysteine to Membranes from Rat Cerebral CortexJournal of Neurochemistry, 1981
- La S-adénosyl-L-homocystéine : 2. AnticonvulsivanteCanadian Journal of Physiology and Pharmacology, 1980
- La S-adénosyl-L-homocystéine : 1. Inductrice de sommeilCanadian Journal of Physiology and Pharmacology, 1980
- Purification de la S-adénosyl-L-homocystéine hydrolase du foie de rat par chromatographie d'affinitéCellular and Molecular Life Sciences, 1979
- BIOSYNTHESIS OF S‐ADENOSYL‐L‐METHIONINE IN THE RAT PINEAL GLANDJournal of Neurochemistry, 1978
- Species and tissue differences in the catabolism of S-adenosyl-L-homocysteine: A quantitative, chromatographic studyLife Sciences, 1977
- Biogenesis of 5‐methoxy‐N,N‐dimethyltryptamine in human pineal glandJournal of Neurochemistry, 1976
- THE FORMATION OF S-ADENOSYLHOMOCYSTEINE IN ENZYMATIC TRANSMETHYLATION REACTIONS1Journal of the American Chemical Society, 1954
- THE NATURE OF THE ACTIVE METHYL DONOR FORMED ENZYMATICALLY FROM L-METHIONINE AND ADENOSINETRIPHOSPHATE1,2Journal of the American Chemical Society, 1952