The molecular mobility of protein in lyophilized lysozyme-sugar systems stored at different relative humidities was studied using solid-state NMR. Relaxation measurements, T(1) of high-frequency (MHz), and T(1rho), of low-frequency (kHz) motions, were performed on lysozyme lyophilized with lactose a
Moisture-induced aggregation of lyophilized proteins in the solid state
β Scribed by W. Robert Liu; Robert Langer; Alexander M. Klibanov
- Publisher
- John Wiley and Sons
- Year
- 1991
- Tongue
- English
- Weight
- 776 KB
- Volume
- 37
- Category
- Article
- ISSN
- 0006-3592
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Purpose: To investigate the effect of plasticizers on the stability of protein formulations in the solid state and to apply these results to a study of mechanisms of protein stabilization by sugars in the solid sate. ## Methods: The igg1 antibody was formulated with either sucrose or trehalose
The solid state is preferred for many proteins due to their marginal stability in solution. However, even in the solid state, chemical and physical degradation can occur on the time scale of the drying process, distribution and use. This review summarizes the major degradation pathways of proteins i