DIHYDROPTERIDINE REDUCTASE FROM SHEEP LI

Purification Methods

Dihydropteridine reductase is purified to homogeneity on a naphthoquinone affinity adsorbent, followed by DEAE-Sephadex and CM-Sephadex chromatography. [Firgaira, Cotton and Danks, Biochem J 197 31 1981.] [For other dihydropteridine reductases see Armarego et al. Med Res Rev 4(3) 267 1984.] 3,4-Dihydroxyphenylalanine-containing proteins. Boronate affinity chromatography is used in the selective binding of proteins containing 3,4-dihydroxyphenylalanine to a m-phenylboronate agarose column and eluted with 1M NH4OAc at pH 10. [Hankus et al. Anal Biochem 150 187 1986.]