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.
| 元の言語 | 英語 |
|---|---|
| ページ（範囲） | 157-161 |
| ページ数 | 5 |
| ジャーナル | kagaku kogaku ronbunshu |
| 巻 | 41 |
| 発行部数 | 2 |
| DOI | |
| 出版物ステータス | 出版済み - 3 20 2015 |
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All Science Journal Classification (ASJC) codes
- Chemistry(all)
- Chemical Engineering(all)
これを引用
Development of a peroxidase-Fused protein reagent by brevibacillus choshinensis heterologous expression system. / Hayashi, Kounosuke; Tomozoe, Yusuke; Nagai, Kenji; Hiraishi, Yoshiyuki; Kamiya, Noriho.
：: kagaku kogaku ronbunshu, 巻 41, 番号 2, 20.03.2015, p. 157-161.研究成果: ジャーナルへの寄稿 › 記事
}
TY - JOUR
T1 - Development of a peroxidase-Fused protein reagent by brevibacillus choshinensis heterologous expression system
AU - Hayashi, Kounosuke
AU - Tomozoe, Yusuke
AU - Nagai, Kenji
AU - Hiraishi, Yoshiyuki
AU - Kamiya, Noriho
PY - 2015/3/20
Y1 - 2015/3/20
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84925328743&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84925328743&partnerID=8YFLogxK
U2 - 10.1252/kakoronbunshu.41.157
DO - 10.1252/kakoronbunshu.41.157
M3 - Article
AN - SCOPUS:84925328743
VL - 41
SP - 157
EP - 161
JO - Kagaku Kogaku Ronbunshu
JF - Kagaku Kogaku Ronbunshu
SN - 0386-216X
IS - 2
ER -