Sedimentation analysis of ribonucleotide reductase activity in extracts of Pseudomonas stutzeri
โ Scribed by Robert G. Holt; Bam D. Mehrotra; Franklin D. Hamilton
- Book ID
- 115758241
- Publisher
- Elsevier Science
- Year
- 1985
- Tongue
- English
- Weight
- 394 KB
- Volume
- 128
- Category
- Article
- ISSN
- 0006-291X
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๐ SIMILAR VOLUMES
Mammalian ribonucleotide reductase catalyzes the rate-limiting for the de novo synthesis 2'-deoxyribonucleoside 5'-triphosphates. There is some suggestion that this step may also be the rate-limiting step of DNA synthesis. It is apparent that the level of the enzyme, ribonucleotide reductase, varies
Determination of ribonucleotide reductase (EC 1.17.4.1) activity in plant extracts requires the optimum resolution of substrate and product in the radioactive enzyme assay. By ion exclusion or ion-exchange chromatography of nucleoside 5'monophosphates or nucleosides, respectively, on cation-exchange