Kinetics of formation and dissociation of manganese-bovine carbonic anhydrase B
β Scribed by Wilkins, Ralph G.; Williams, Kathryn R.
- Book ID
- 127280130
- Publisher
- American Chemical Society
- Year
- 1974
- Tongue
- English
- Weight
- 611 KB
- Volume
- 96
- Category
- Article
- ISSN
- 0002-7863
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π SIMILAR VOLUMES
The kinetics of dissociation of Zn 2+ from the metalloenzyme carbonic anhydrase was measured over a range of pH, temperature, and acetate concentration. The rate of dissociation is extremely slow at neutral pH (tl/2 ~ 3 years, 4Β°C), but increases in almost direct proportion to the hydrogen ion conce
## Abstract We have attempted to elucidate the mechanism of the acquisition of activeβsite conformation in enzymes by studying the unfolding and refolding of Co(II) carbonic anhydrase. This enzyme possesses characteristic absorption and CD spectra in the visible region, which reflect primarily the