𝔖 Bobbio Scriptorium
✦   LIBER   ✦

State of aggregation of recombinant hirudin in solution under physiological conditions

✍ 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.


πŸ“œ SIMILAR VOLUMES


Copper-glutathione complexes under physi
✍ Jens Z. Pedersen; Christian SteinkΓΌhler; Ulrich Weser; Giuseppe Rotilio πŸ“‚ Article πŸ“… 1996 πŸ› Springer Netherlands 🌐 English βš– 581 KB

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

Aggregation of recombinant human botulin
✍ Shujun Bai; Mark Cornell Manning; Theodore W. Randolph; John F. Carpenter πŸ“‚ Article πŸ“… 2011 πŸ› John Wiley and Sons 🌐 English βš– 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