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• W192690905 abstract "A soluble enzyme preparation catalysing the release of adenine from 5′-methylthioadenosine was purified some 30-fold from extracts of the rat ventral prostate. This reaction was completely dependent on addition of inorganic phosphate ions to the assay medium. This absolute requirement for phosphate ions suggests a phosphorolytic cleavage mechanism. After acid treatment, the other product of the reaction appeared to be 5-methylthioribose. The actions of some other well-characterized enzymes of nucleoside metabolism of 5′-methylthioadenosine were also investigated; purified purine nucleoside phosphorylases from calf spleen and human erythrocytes did not attack 5′-methylthioadenosine. The role of 5′-methylthioadenosine in mammalian tissues is discussed." @default.
• W192690905 created "2016-06-24" @default.
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• W192690905 date "1969-11-01" @default.
• W192690905 modified "2023-10-09" @default.
• W192690905 title "Phosphate-stimulated breakdown of 5′-methylthioadenosine by rat ventral prostate" @default.
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• W192690905 doi "https://doi.org/10.1042/bj1150241" @default.
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