Renaturation of recombinant secretory leukocyte protease inhibitor : aspects of disulfide bond formation kinetics

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....

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Bibliographic Details
Published inBiotechnology letters Vol. 15; no. 9; pp. 943 - 948
Main Authors HARCUM, S. W, DALE, B. E, SEELY, R. J
Format Journal Article
LanguageEnglish
Published Dordrecht Springer 01.09.1993
Subjects
Biological and medical sciences
Biotechnology
Enzyme engineering
Escherichia coli
Fundamental and applied biological sciences. Psychology
Methods. Procedures. Technologies
Miscellaneous
Temperature
Enzyme
Leukocyte
Disulfide bond
Secretion
Hydrolases
Environmental factor
Kinetics
Inhibition
Recombinant protein
Activation energy
Proteinases
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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).
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
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ISSN:0141-5492
1573-6776
DOI:10.1007/BF00131761