A Naphthoquinone Adsorbent for Affinity Chromatography of Human Dihydropteridine Reductase
- 1 February 1978
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 83 (1), 319-324
- https://doi.org/10.1111/j.1432-1033.1978.tb12097.x
Abstract
A 1,2-naphthoquinone adsorbent is described which allows simple purification of [human and Macaca irus liver] dihydropteridine reductase [EC 1.6.99.7] directly from crude extract. The native MW indicates that a tetramer structure of the species is isolated by this method; this is unusual and possibly reflects the capacity of the procedure to preserve the native state of the enzyme.This publication has 11 references indexed in Scilit:
- Dihydropteridine Reductase from Bovine LiverThe Journal of Biochemistry, 1977
- Purification of inactive phenylalanine hydroxylase protein from liver in classical phenylketonuriaNature, 1976
- Phenylalanine Hydroxylase of Macaca irusEuropean Journal of Biochemistry, 1975
- Phenylketonuria Due to a Deficiency of Dihydropteridine ReductaseNew England Journal of Medicine, 1975
- Proceedings: Atypical phenylketonuria accompanied by a severe progressive neurological illness unresponsive to dietary treatment.Archives of Disease in Childhood, 1974
- Properties of Purified Quinonoid Dihydropterin ReductaseCanadian Journal of Biochemistry, 1973
- Dihydrofolate Reductase of Streptococcus faeciumPublished by Elsevier ,1968