The Isolation and Characterization of Dihydropteridine Reductase from Sheep Liver

作者: Jonathan E. Craine , E. Stanley Hall , Seymour Kaufman

DOI: 10.1016/S0021-9258(19)44767-4

关键词:

摘要: Abstract Dihydropteridine reductase has been obtained from sheep liver in essentially homogeneous form. The enzyme exists as a dimer of molecular weight 41,000 to 42,800. subunit determined be 21,300. In the presence quinonoid tautomer either dihydrobiopterin or dihydro-6, 7-dimethylpterin, DPNH is better substrate than TPNH. Evidence indicates that activity this far greater known pterindependent hydroxylases all tissues examined.

参考文章(43)
Sidney Futterman, ENZYMATIC REDUCTION OF FOLIC ACID AND DIHYDROFOLIC ACID TO TETRAHYDROFOLIC ACID Journal of Biological Chemistry. ,vol. 228, pp. 1031- 1038 ,(1957) , 10.1016/S0021-9258(18)70678-9
G.H. Beaven, E.R. Holiday, Ultraviolet absorption spectra of proteins and amino acids. Advances in Protein Chemistry. ,vol. 7, pp. 319- 386 ,(1952) , 10.1016/S0065-3233(08)60022-4
Seymour Kaufman, Daniel B. Fisher, Purification and Some Physical Properties of Phenylalanine Hydroxylase from Rat Liver Journal of Biological Chemistry. ,vol. 245, pp. 4745- 4750 ,(1970) , 10.1016/S0021-9258(18)62856-X
Seymour Kaufman, A Protein That Stimulates Rat Liver Phenylalanine Hydroxylase Journal of Biological Chemistry. ,vol. 245, pp. 4751- 4759 ,(1970) , 10.1016/S0021-9258(18)62857-1
M.J. Osborn, F.M. Huennekens, Enzymatic Reduction of Dihydrofolic Acid Journal of Biological Chemistry. ,vol. 233, pp. 969- 974 ,(1958) , 10.1016/S0021-9258(18)64688-5
Seymour Kaufman, A NEW COFACTOR REQUIRED FOR THE ENZYMATIC CONVERSION OF PHENYLALANINE TO TYROSINE Journal of Biological Chemistry. ,vol. 230, pp. 931- 939 ,(1958) , 10.1016/S0021-9258(18)70516-4
Seymour Kaufman, Studies on the mechanism of the enzymatic conversion of phenylalanine to tyrosine. Journal of Biological Chemistry. ,vol. 234, pp. 2677- 2682 ,(1959) , 10.1016/S0021-9258(18)69758-3