The binding of thiophenols to bovine carbonic anhydrase
β Scribed by Jitka Olander; E.T. Kaiser
- Book ID
- 118852586
- Publisher
- Elsevier Science
- Year
- 1971
- Tongue
- English
- Weight
- 286 KB
- Volume
- 45
- Category
- Article
- ISSN
- 0006-291X
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The affinity of bicarboxylate ions (from oxaiate to glutarate) for cobalt(E) bovine carbonic anhydrase has been investigated and compared with that cf acetate and propionate. The oxalate ion shows a much greater affiiity for the enzyme than acetate. whereas the other bicarboxylate ions have very lit
## Abstract A practical laboratory experiment is described that illustrates the application of fluorescence resonance energy transfer to the study of proteinβligand binding. The affinities of wildβtype and mutant human carbonic anhydrase II for dansylamide were determined by monitoring the increase