[5'-methylthioadenosine phosphorylase from the human prostate. 1. Purification and partial characterization].
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.
D000241:Adenosine / Q000031:analogs & derivatives; D006801:Humans; D008297:Male; D010430:Pentosyltransferases / Q000302:isolation & purification*; D011467:Prostate / Q000201:enzymology*; D011683:Purine-Nucleoside Phosphorylase / Q000032:analysis / Q000302:isolation & purification*; D013872:Thionucleosides
D013872:Thionucleosides; D010430:Pentosyltransferases; D011683:Purine-Nucleoside Phosphorylase; C021784:5'-methylthioadenosine phosphorylase; D000241:Adenosine
5'-metiltioadenosina fosforilasi da prostata umana. 1. Purificazione e parziale caratterizzazione.