抄録
To detect a target protein in biological samples, a fusion protein was designed composed of a peroxidase from Arthromyces ramosus (ARP) and parts of the antibody-binding domains of Staphylococcus aureus protein A and Streptococcus protein G (PG). The ARP-PG fusion protein was successfully expressed by a heterologous protein expression system in Brevibacillus choshinensis. The fusion protein was secreted as an active form in culture media. The production of ARP-PG with higher peroxidase activity was observed by the addition of 5-aminolevulinic acid to the culture media. The performance of purified ARP-PG was validated by dot blotting for the detection of transferrin as a model target protein. A comparable performance in the dot blot analysis was attained using a culture supernatant containing crude but active ARP-PG, indicating the practicality of the Brevibacillus protein secretion system.
本文言語 | 英語 |
---|---|
ページ(範囲) | 157-161 |
ページ数 | 5 |
ジャーナル | kagaku kogaku ronbunshu |
巻 | 41 |
号 | 2 |
DOI | |
出版ステータス | 出版済み - 3月 20 2015 |
!!!All Science Journal Classification (ASJC) codes
- 化学 (全般)
- 化学工学(全般)