| Literature DB >> 5378381 |
A E Pegg, H G Williams-Ashman.
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.Entities:
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Year: 1969 PMID: 5378381 PMCID: PMC1185095 DOI: 10.1042/bj1150241
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857