In SituMicroassay of Ornithine Decarboxylase
✍ Scribed by C. Lobo; I.Núñez de Castro; F.J. Alonso
- Publisher
- Elsevier Science
- Year
- 1996
- Tongue
- English
- Weight
- 77 KB
- Volume
- 238
- Category
- Article
- ISSN
- 0003-2697
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Crystals of truncated (A425-461) pyridoxal-5'-phosphate (PLP)-dependent mouse ornithine decarboxylase (mOrnDC') have been obtained that diffract to 2.2 resolution (P2,2,2, a = 119.5 A, b = 74.3 A, c = 46.1 A). OrnDC produces putrescine, which is the precursor for the synthesis of polyamines in eukar
## BACKGROUND. Ornithine decarboxylase (ODC) is a key rate-limiting enzyme in polyamine biosynthesis. Several studies using an enzyme assay revealed that the ODC activity was higher in tumor tissue than in normal tissue. However, there is little information on the mRNA status of ODC in surgical sp