| Autor: |
Shibui, Tatsurou, Uchida-Kamizono, Michiru, Takizawa, Yasuko, Kondo, Jun, Hiyoshi, Chiharu, Murayama, Satoru, Morimoto, Yuuki, Teranishi, Yutaka |
| Zdroj: |
Applied Microbiology & Biotechnology; 1989, Vol. 31 Issue 5/6, p518-523, 6p |
| Abstrakt: |
A gene coding human proapolipoprotein A-I (proapo A-I) was inserted into a plasmid with a consensus ribosome binding sequence in Escherichia coli. One to three copies of this gene were tandemly inserted to construct proapo A-I expression plasmids, pMTpAI, pMT(pAI) and pMT(pAI), respectively. The cells harbouring pMT(pAI), could produce proapo A-I at a level of 49 μg/ml A and up to approx. 48% of the total cellular protein. The product was soluble in E. coli, and formed protein-lipid complexes with dimyristoyl phosphatidyl choline, which formed stacked disc structures. Analyses of the rec proapo A-I formed in the bacteria was identical to human proapo A-I except for methionine at the N-terminus. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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