ISSN:
1573-6776
Source:
Springer Online Journal Archives 1860-2000
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Summary Therapeutic proteins produced in procaryotic hosts often contain disulfide bonds, which must be fully formed to satisfy United States Food and Drug Administration regulations. Native secretory leukocyte protease inhibitor (SLPI), a possible emphysema therapeutic agent, contains many disulfide bonds. However, when SLPI is produced in Escherichia coli by rDNA technology, the disulfide bonds are not formed correctly and must be generated by in vitro renaturation. In this study, the reaction rate parameters were estimated for SLPI renaturation. The apparent activation energy was approximately 5 kcal/mol suggesting that renaturation is a diffusion limited process. Apparent reaction rate orders were not constant, suggesting complex renaturation mechanism(s).
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00131761
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