5'-methylthioadenosine phosphorylase from the human prostate. 1. Purification and partial characterization
Oliva, A.; Cacciapuoti, G.; Galletti, P.; Porcelli, M.; Zappia, V.
Bollettino della Societa Italiana di Biologia Sperimentale 54(21): 2091-2097
1978
ISSN/ISBN: 0037-8771 PMID: 109102 Document Number: 135399
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.