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In Vitro and In Vivo Binding of S ‐Adenosyl‐L‐Homocysteine to Membranes from Rat Cerebral Cortex
Author(s) -
Fonlupt P.,
Rey C.,
Pacheco H.
Publication year - 1981
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1981.tb02391.x
Subject(s) - adenosine , membrane , cerebral cortex , in vivo , biochemistry , in vitro , binding site , receptor , chemistry , methionine , adenosine triphosphate , biology , amino acid , endocrinology , microbiology and biotechnology
Membranes from rat cerebral cortex are able to bind S ‐adenosyl‐L‐homocysteine (SAH) with a K D of 5. 10 ‐7 M and n of 170 pmol/g fresh tissue (i.e. 20 mg protein). The binding is enhanced by Mg 2+ and Ca 2‐ but not K + and Na + , γ‐Aminobutyric acid, diazepine, noradrenaline and a antagonists are without any effect; S ‐adenosyl‐L‐methionine, adenosine and adenosine triphosphate inhibit SAH binding. Linkage with an adenosine receptor has not been expressly demonstrated by our method. SAH binding proteins are more abundant in the crude synaptosomal pellet (P 2 ). A similar fixation seems to occur on brain membranes after [ 3 H]SAH administration to rat. The binding might be linked to a methylase activity or an adenosine receptor.