Stability of crystalline proteins
| Autor: | Weizhong Shan, Bhami C. Shenoy, Alexey L. Margolin, Yi Wang |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Chromatography
biology Chemistry Infrared spectroscopy Bioengineering Crystal structure Applied Microbiology and Biotechnology Protein Structure Secondary Amorphous solid Glucose Oxidase Spectroscopy Fourier Transform Infrared Chromatography Gel biology.protein Native state Biophysics Glucose oxidase sense organs Lipase Crystallization Protein crystallization Protein secondary structure Chromatography High Pressure Liquid Biotechnology |
| Zdroj: | Biotechnology and Bioengineering. 73:358-369 |
| ISSN: | 1097-0290 0006-3592 |
| DOI: | 10.1002/bit.1069 |
| Popis: | By using two model proteins, glucose oxidase and lipase, we demonstrate that dry crystalline formulations are significantly more stable than their amorphous counterparts. The results of Fourier-transform infrared spectroscopy indicate that crystalline proteins better maintain their native conformation in accelerated stability studies. The lower tendency of crystalline proteins to aggregate is confirmed by size-exclusion chromatography. The data suggest that protein crystallization may significantly improve some aspects of protein handling, and change the way biopharmaceuticals are produced, formulated, and delivered. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text