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- W2051334564 abstract "1 A 423-fold purified fraction of uroporphyrinogen decarboxylase (EC 4.1.1.37) showing a specific activity of 770 units/mg protein has been employed in order to study some properties in etiolated Euglena gracilis Z. 2 Uroporphyrinogen decarboxylase has a relative molecular mass of 54000, an optimum pH of 7.2 and exhibits Michaelis-Menten kinetics, employing both uroporphyrinogen I and uroporphyrinogen III as substrates. 3 Anaerobic conditions seem not to be necessary for uroporphyrinogen decarboxylase activity. Neither EDTA nor cysteine affected enzyme activity, whereas dithiothreitol produced a remarkable activation of coproporphyrinogen formation. 4 Kinetic data employing both substrates showed an accumulation of porphyrinogen (i.e. hexa- and heptaporphyrin) containing six or seven COOH groups, depending on the uroporphyrinogen concentration used. 5 An unusual elution profile of the intermediates on Sephacryl S-200 was found." @default.
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- W2051334564 date "1989-02-01" @default.
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- W2051334564 title "Studies on uroporphyrinogen decarboxylase of etiolated Euglena gracilis Z" @default.
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- W2051334564 doi "https://doi.org/10.1111/j.1432-1033.1989.tb14570.x" @default.
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