ブレビバチルス発現系によるペルオキシダーゼ融合タンパク質試薬の調製

Translated title of the contribution: Development of a Peroxidase-Fused Protein Reagent by <i>Brevibacillus choshinensis</i> Heterologous Expression System

林 浩之輔, 友添 祐介, 永井 賢治, 平石 佳之, 神谷 典穂

Research output: Contribution to journalArticlepeer-review

Abstract

To detect a target protein in biological samples, a fusion protein was designed composed of a peroxidase from <i>Arthromyces ramosus</i> (ARP) and parts of the antibody-binding domains of <i>Staphylococcus aureus</i> protein A and <i>Streptococcus</i> protein G (PG). The ARP-PG fusion protein was successfully expressed by a heterologous protein expression system in <i>Brevibacillus choshinensis</i>. 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 <i>Brevibacillus</i> protein secretion system.
Translated title of the contributionDevelopment of a Peroxidase-Fused Protein Reagent by <i>Brevibacillus choshinensis</i> Heterologous Expression System
Original languageJapanese
Pages (from-to)157-161
Number of pages5
JournalKagaku Kogaku Ronbunshu
Volume41
Issue number2
DOIs
Publication statusPublished - 2015

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