| Autor: |
Hayden, M., Traphagen, L., Wilkins, J., Schmitz, E., Laird, D., Herrmann, R., Mandecki, W. |
| Zdroj: |
Protein Expression and Purification; June 1995, Vol. 6 Issue: 3 p256-264, 9p |
| Abstrakt: |
The human cardiac troponin I gene was subcloned and expressed at high levels in Escherichia coli as a fusion protein to CMP-KDO synthetase (CKS). Expression levels of the CKS-troponin I fusion were 8% of total cellular protein 4 h after induction with IPTG. The fusion was expressed primarily as an insoluble protein as shown by SDS-PAGE analysis. Expressed CKS-troponin I fusion from a crude lysate was antigenic against anti-CKS and anti-troponin I monoclonal antibodies in Western blots. The fusion was affinity-purified over a TnC affinity column using a urea-solubilized extract of a crude cell lysate. Serial dilutions of crude soluble extracts of the troponin I fusion were assayed in several microparticle enzyme immunoassays and found to exhibit similar immunogenic responses relative to cardiac troponin I isolated from human heart tissue.Copyright 1995, 1999 Academic Press, Inc. |
| Databáze: |
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