The physiologically important copper complexes of oxidized glutathione have been examined by electron spin resonance (ESR) spectroscopy in aqueous solution at neutral pH. Low temperature measurements show that the Cu(ll) binding site in oxidized glutathione has the same ligand arrangement as in the
β¦ LIBER β¦
State of aggregation of recombinant hirudin in solution under physiological conditions
β Scribed by Theodore W. Thannhauser; Harold A. Scheraga
- Book ID
- 105390186
- Publisher
- Springer
- Year
- 1996
- Tongue
- English
- Weight
- 237 KB
- Volume
- 15
- Category
- Article
- ISSN
- 1573-4943
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
Copper-glutathione complexes under physi
β
Jens Z. Pedersen; Christian SteinkΓΌhler; Ulrich Weser; Giuseppe Rotilio
π
Article
π
1996
π
Springer Netherlands
π
English
β 581 KB
Studies in Mass Physiology: The Activity
β
Frank Schuett
π
Article
π
1934
π
Ecological Society of America
π
English
β 435 KB
Chemical Degradation Kinetics of Recombi
β
Ursula Gietz; Ruth Alder; Peter Langguth; Tudor Arvinte; Hans P. Merkle
π
Article
π
1998
π
Springer US
π
English
β 573 KB
Aggregation of Granulocyte Colony Stimul
β
Krishnan, Sampathkumar; Chi, Eva Y.; Webb, Jonathan N.; Chang, Byeong S.; Shan,
π
Article
π
2002
π
American Chemical Society
π
English
β 111 KB
Aggregation and disaggregation of Aeromo
β
Xiaojuan Xu; Lina Zhang
π
Article
π
2000
π
John Wiley and Sons
π
English
β 153 KB
π 2 views
Aggregation of recombinant human botulin
β
Shujun Bai; Mark Cornell Manning; Theodore W. Randolph; John F. Carpenter
π
Article
π
2011
π
John Wiley and Sons
π
English
β 460 KB
Solution conditions greatly affect the aggregation rate of a protein. Elucidating these influences provides insight into the critical factors governing aggregation. In this study, recombinant human botulinum protein antigen serotype C [rBoNTC (H(c))] was employed as a model protein. rBoNTC (H(c)) ag