title: Purification and characterization of 5'-deoxy-5'-methylthioadenosine (MTA) phosphorylase from human liver.
abstract: 5'-Methylthioadenosine phosphorylase was purified 8000-fold from human liver using a combination of affinity chromatography, chromatofocusing and gel filtration. A 25% overall yield was obtained. The specific activity of the final preparation was 40 mumol of 5'-methylthioadenosine cleaved per hr per mg of protein. The enzyme had an apparent molecular weight of 55,000 daltons, as determined by gel filtration of Superose 12 and Sephadex G-150, with a subunit molecular weight of 30,000 daltons, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The substrate specificity of the purified enzyme was studied in both the direction of nucleoside cleavage and nucleoside synthesis.
authors.affiliation: Wellcome Research Laboratories, Research Triangle Park, NC 27709.
authors.forename: D
authors.initials: D
authors.lastname: Toorchen
authors.forename: R L
authors.initials: RL
authors.lastname: Miller
mesh_terms: D002850:Chromatography, Gel; D006801:Humans; D008099:Liver / Q000737:chemistry / Q000201:enzymology*; D009705:Nucleosides / Q000096:biosynthesis / Q000378:metabolism; D011683:Purine-Nucleoside Phosphorylase / Q000302:isolation & purification* / Q000378:metabolism; D011687:Purines / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D009705:Nucleosides; D011687:Purines; D011683:Purine-Nucleoside Phosphorylase; C021784:5'-methylthioadenosine phosphorylase