[5'-methylthioadenosine phosphorylase from the human prostate. 1. Purification and partial characterization]
- PMID: 109102
[5'-methylthioadenosine phosphorylase from the human prostate. 1. Purification and partial characterization]
Abstract
5'-Methylthioadenosine phosphorylase has been purified approximately 340-fold in 20% yield from human prostate: the use of affinity chromatography by Sepharose-Hg has been found particularly advantageous. The enzyme has been partially characterized and an apparent Km of 2.5 x 10(-5) M has been calculated for 5'-methylthioadenosine. The reaction is activated by thiols and shows an absolute requirement for phosphate ions.
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