| Autor: |
Parente, Dino, Raucci, Giuseppe, D'Alatri, Laura, d'Estais, Guy, Novelli, Sabrina, Pacilli, Aurelio, Saccinto, Maria, Mele, Antonio, Santis, Rita |
| Zdroj: |
Molecular Biotechnology; Apr1998, Vol. 9 Issue 2, p99-106, 8p |
| Abstrakt: |
The goal of the present study was to establish the condition to obtain preparative amounts of the recombinant cytotoxin α-sarcin to be used for immunoconjugate production. α-Sarcin cDNA was isolated from Aspergillus giganteus strain MDH 18894 and its expression in Escherichia coli was attempted by the use of both two-cistron and fusion protein-expression systems. Whereas the former resulted in low intracellular expression level of recombinant α-sarcin (r-Sar), the latter allowed high-level expression of the fusion protein in the culture supernant. A variant form of α-sarcin with an additional threonine residue in position 1 (Thr-Sar) was obtained by proteolytic processing of the fusion protein with a final yield after purification of 40 mg/L of culture. Both recombinant proteins r-Sar and Thr-Sar were identical to native a-sarcin with respect to the biochemical properties and to the in vitro biological activity. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
Full text from SpringerLink