BUCHNER, J and RUDOLPH, R (1991) RENATURATION, PURIFICATION AND CHARACTERIZATION OF RECOMBINANT FAB-FRAGMENTS PRODUCED IN ESCHERICHIA-COLI. BIO-TECHNOLOGY, 9 (2). pp. 157-162. ISSN 0733-222X,
Full text not available from this repository.Abstract
Cytoplasmatic expression of murine antibody chains in Escherichia coli results in the formation of insoluble and inactive protein aggregates (inclusion bodies). By systematic variation of the parameters influencing the folding, formation of disulfide bonds and association of the constituent polypeptide chains, we have designed a renaturation procedure allowing the production of microbially expressed F(ab)-fragments at yields up to 40 percent of the total amount of recombinant protein. The strategy of optimization is generally applicable for disulfide containing proteins produced as inclusion bodies in bacteria. The purified recombinant antibody fragments obtained are identical with the native murine F(ab) in all functional and physicochemical parameters tested.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | LACTIC-DEHYDROGENASE; LIGHT-CHAIN; PROTEINS; REACTIVATION; ANTIBODY; AGGREGATION; DISULFIDE; HEAVY; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:46 |
| URI: | https://pred.uni-regensburg.de/id/eprint/55088 |
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