کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1975304 | 1060614 | 2013 | 7 صفحه PDF | دانلود رایگان |
We purified d-amino acid oxidase (EC 1.4.3.3, DAO) from Xenopus laevis tadpoles. The optimal temperature and pH for enzyme activity were 35–40 °C and 8.3–9.0, respectively, depending on the substrate amino acids available to the enzyme; the highest activity was observed with d-proline followed by d-phenylalanine. Activity was significantly inhibited by p-hydroxymercuribenzoate, but only moderately by p-chloromercuribenzoate or benzoate. Enzyme activity was increased until the final tadpole stage, but was reduced to one-third in the adult and was localized primarily in the kidney. The tadpoles contained high concentrations of d-proline close to the final developmental stage and nearly no d-amino acids were detected in the adult frog, indicating that d-amino acid oxidase functions in metamorphosis.
Journal: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology - Volume 166, Issue 2, October 2013, Pages 165–171