Purification and characterization of 5'-deoxy-5'-methylthioadenosine (MTA) phosphorylase from human liver

Biochemical Pharmacology
D Toorchen, R L Miller

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.

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Citations

May 28, 1992·Biochemical Pharmacology·R T SmolenskiH A Simmonds
Aug 9, 2011·Journal of Bacteriology·Kajal BuckoreelallWilliam B Parker
Jan 10, 2012·Tuberculosis·Kajal BuckoreelallWilliam B Parker
Jan 29, 2016·Molecular & Cellular Proteomics : MCP·Emilie Bigaud, Fernando J Corrales
Jun 15, 2014·The Oncologist·Pashna N MunshiJoseph R Bertino

Related Concepts

5'-Methylthioadenosine phosphorylase
Molecular Sieve Chromatography
Liver
Nucleosides
Nicotinamide Riboside Phosphorylase
Purines
Substrate Specificity

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