Abstract:
:A 100-fold purification of a reduced triphosphopyridine nucleotide/3-methyleneoxindole reductase of peas has been achieved using conventional protein fractionation procedures. Reduced diphosphopyridine nucleotide is 25-fold less effective than reduced triphosphopyridine nucleotide as the reductant. The preparation is free of other reductase activities including those linking the oxidation of reduced pyridine nucleotide coenzymes to the reduction of cytochrome c; vitamins K(1), K(2), and K(3); O(2); nitrate; oxidized glutathione; and thiazolyl blue tetrazolium. The affinity of the enzyme for 3-methyleneoxindole (K(s) = 0.5 mm 3-methyleneoxindole) is relatively high. It is, therefore, reasonable to assume that 3-methyleneoxindole is the normal substrate.The enzyme is inhibited by indole-3-acetic acid, indole-3-aldehyde, and by l-naph-thaleneacetic acid. While these are not especially powerful inhibitors (K(1) = 1.9-4.0 mm) the competitive relationship with 3-methyleneoxindole indicates that significant inhibition might occur at low intracellular concentrations of the substrate.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
Moyed HS,Williamson Vdoi
10.1104/pp.42.4.510subject
Has Abstractpub_date
1967-04-01 00:00:00pages
510-4issue
4eissn
0032-0889issn
1532-2548journal_volume
42pub_type
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