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. 1978 Nov 15;54(21):2091-7.

[5'-methylthioadenosine phosphorylase from the human prostate. 1. Purification and partial characterization]

[Article in Italian]
A Oliva, G Cacciapuoti, P Galletti, M Porcelli, V Zappia
  • PMID: 109102

[5'-methylthioadenosine phosphorylase from the human prostate. 1. Purification and partial characterization]

[Article in Italian]
A Oliva et al. Boll Soc Ital Biol Sper. .

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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