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1 N-Terminal sequence analysis of the gel- purified enzyme gave a single, serine-rich sequence.
2 Recombinant hMYH has essentially similar activities to the partially purified enzyme .
3 To test the model, the branch-point was reconstituted with purified enzymes .
4 NADPH-cytochrome c reductase activity increased by 95-fold in the purified enzyme .
5 Both purified enzymes showed allergenic activity in the mediator release assay.
6 The purified enzyme shows no detectable activity in the in vitro selenophosphate synthetase assay.
7 The purified enzyme also can transfer a phosphate from bis-PP-IP4 to ADP to form ATP.
8 The kinetic constants of the purified enzymes were similar to those reported for other purification methods.
9 The biosynthetic pathways to a number of natural products have been reconstituted in vitro using purified enzymes .
10 The molecular mass of the purified enzyme was 113 kDa, as determined by SDS-PAGE under reducing conditions.
11 The purified enzyme is a dimer containing an iron-sulfur cluster and displays activity in in vitro assays.
12 The activity of these purified enzymes has been compared with the wild-type enzyme expressed in mammalian cells.
13 The molecular weight of the purified enzyme was estimated 70,000 by SDS-PAGE.
14 The purified enzyme catalyzed the dehydrogenation of various d-amino acids, with d-phenylalanine being the most preferred substrate.
15 The purified enzyme was further characterized with respect to substrate specificity, kinetic parameters and amino terminal sequence.
16 The purified enzyme is a monomer with two iron atoms and displays activity in in vitro assays.
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