[11] Orotidylate decarboxylase (yeast)
作者： A. Yoshimoto , K. Umezu , K. Kobayashi , K. Tomita
DOI: 10.1016/S0076-6879(78)51013-6
关键词: Uridine monophosphate 、 Chromatography 、 Biochemistry 、 Enzyme 、 Yeast 、 Sodium dodecyl sulfate 、 Chemistry 、 Ethylenediaminetetraacetic acid 、 Absorbance 、 Enzyme assay 、 Polyacrylamide gel electrophoresis
摘要: Publisher Summary This chapter describes the purification procedure of orotidylate decarboxylase enzyme form yeast. A spectrophotometric assay, based on formation uridine monophosphate (UMP) from orotidylate, is employed. The reaction followed by decrease in absorbance at 285 nm. purified hydroxylapatite almost homogeneous polyacrylamide gel electrophoresis but still contains a minute amount faster moving band; main protein band coincides with that activity. When denatured and reduced subjected to presence sodium dodecyl sulfate, two bands appear; molecular weight estimated be 26,000 faint minor (probably undissociated protein) 50,000. activity yeast optimal pH 5.5. Uridine nucleotides Ethylenediaminetetraacetic acid (EDTA) show no inhibition standard assay.
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