Properties of Purified Quinonoid Dihydropterin Reductase
1973 ◽
Vol 51
(9)
◽
pp. 1229-1239
◽
Keyword(s):
Quinonoid dihydropterin reductase has been purified to homogeneity from sheep liver, sheep brain, and beef adrenal medulla. Each of these enzymes has a molecular weight of about 45 000–55 000, and is composed of two subunits of half that weight. The subunits of the sheep liver reductase have identical charge, size, and N-terminal amino acid residue. The reductase exists in solution over a wide range of concentrations as the dimer. A dimer covalently linked by dimethylsuberimidate retains full activity. A number of kinetic properties of quinonoid dihydropterin reductase, including inhibition by thiol reagents and by pterin analogues, are reported.
1970 ◽
Vol 36
(2)
◽
pp. 229-240
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1984 ◽
Vol 788
(1)
◽
pp. 23-34
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1968 ◽
Vol 23
(11)
◽
pp. 1412-1426
◽
1970 ◽
Vol 48
(9)
◽
pp. 1017-1021
◽
1970 ◽
Vol 34
(2)
◽
pp. 289-295
Keyword(s):
Keyword(s):
1970 ◽
Vol 34
(2)
◽
pp. 289-295
◽
Keyword(s):