
doi: 10.1139/o65-022
pmid: 14325967
An enzyme, probably benzimidazole nucleotide:pyrophosphate phosphoribosyl transferase, has been demonstrated in the 33–65% (NH4)2SO4fraction of wheat embryos. The enzyme was assayed indirectly by the apparent inhibition of the analogous orotidine-5′-phosphate pyrophosphorylase caused by benzimidazole competing with orotate for P-ribosyl-PP. Both enzymes were in the same fraction. The reaction product, benzimidazole nucleotide, was separated by paper electrophoresis and thin-layer and column chromatography, and was identified by chemical and spectral analysis. Kinetin showed similar competitive behavior.
Diphosphates, Electrophoresis, Orotic Acid, Chromatography, Metabolism, Glucosyltransferases, Nucleotides, Spectrophotometry, Ultraviolet Rays, Research, Benzimidazoles, Triticum
Diphosphates, Electrophoresis, Orotic Acid, Chromatography, Metabolism, Glucosyltransferases, Nucleotides, Spectrophotometry, Ultraviolet Rays, Research, Benzimidazoles, Triticum
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