VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Purification and properties of the serotonin-stimulated adenylate deaminase from the mitochondrial fraction of rat liver

   
Gridneva L.I., Suvorov N.N., Gorkin V.Z.
PubMed Id: 16394
Year: 1976  Volume: 22  Issue: 2  Pages: 245-254
A method is described for partial purification of structurally bound adenilate desaminase from rat liver tissue mitochondria; the enzyme was stimulated by parenteral administration of serotonine. The enzymatic preparations obtained desaminated AMP, 2',3'-AMP and adenosine, but they did not effect on ATP, 2',3'-cycloAMP or 3',5'-cycloAMP. The maximal rate of desaminating of these substances by AMP-desaminase, stimulated with serotonine, exceeded approximately 1.4-fold the same values, which were obtained for the enzymatic preparations from liver tissue mitochondria of rats, administered with physiological solution. Mitochondrial serotomine-stimulated adenilate desaminase was differentiated from the other soluble adenilate desaminases by some properties; the enzyme was likely to participate also in the regulation of nucleotides balance in the organism.
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Gridneva, L. I., Suvorov, N. N., Gorkin, V. Z. (1976). Purification and properties of the serotonin-stimulated adenylate deaminase from the mitochondrial fraction of rat liver. Voprosy Meditsinskoi Khimii, 22(2), 245-254.
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