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Stability of crystalline proteins
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 conformati...
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Published in: | Biotechnology and bioengineering 2001-06, Vol.73 (5), p.358-369 |
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container_end_page | 369 |
container_issue | 5 |
container_start_page | 358 |
container_title | Biotechnology and bioengineering |
container_volume | 73 |
creator | Shenoy, Bhami Wang, Yi Shan, Weizhong Margolin, Alexey L. |
description | 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. © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 73: 358–369, 2001. |
doi_str_mv | 10.1002/bit.1069 |
format | article |
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subjects | Biological and medical sciences Biotechnology Chromatography, Gel Chromatography, High Pressure Liquid crystalline proteins Crystallization drug formulation Fundamental and applied biological sciences. Psychology Glucose Oxidase - chemistry Health. Pharmaceutical industry Industrial applications and implications. Economical aspects Miscellaneous protein crystals protein stability Protein Structure, Secondary Spectroscopy, Fourier Transform Infrared |
title | Stability of crystalline proteins |
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