A chemically modified glass surface that facilitates transglutaminase- mediated protein immobilization

Yusuke Tanaka, Satoshi Doi, Noriho Kamiya, Noriyuki Kawata, Shinji Kamiya, Kenichi Nakama, Masahiro Goto

研究成果: Contribution to journalArticle査読

7 被引用数 (Scopus)

抄録

An amino-modified glass surface for enzymatic protein immobilization by microbial transglutaminase (MTG) was developed. Diamine substrates with secondary amino groups in the linker moiety, like triethylenetetramine (TETA), exhibited at most a 2-fold higher reactivity in the MTG-catalyzed reaction compared to those with the alkyl linker. A 96-well glass plate was subsequently modified with selected diamine substrates. Validation of the modified surface by enzymatic immobilization of enhanced green fluorescent protein tagged with a glutamine donor-substrate peptide (LLQG) of MTG revealed that the protein loading onto the TETA-modified glass surface was approximately 15-fold higher than that on the unmodified one.

本文言語英語
ページ(範囲)1025-1029
ページ数5
ジャーナルBiotechnology letters
30
6
DOI
出版ステータス出版済み - 6 2008

All Science Journal Classification (ASJC) codes

  • バイオテクノロジー
  • バイオエンジニアリング
  • 応用微生物学とバイオテクノロジー

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