Tetramer formation of a variant type human transthyretin (prealbumin) produced by Escherichia coli expression system

Hirokazu Furuya, Masamitsu Nakazato, Maria Joao Mascarenhas Saraiva, Pedro P. Costa, Hiroyuki Sasaki, Hisayuki Matsuo, Ikuo Goto, Yoshiyuki Sakaki

研究成果: Contribution to journalArticle査読

12 被引用数 (Scopus)

抄録

A variant of human transthyretin(TTR, prealbumin) with methionine for valine substitution at position 30 is a major component of amyloid fibrils found in patients of familial amyloidotic polyneuropathy(FAP) type I, an autosomal dominant genetic disease. But the molecular nature of the variant TTR has been obscure, because most of plasma TTR from FAP patients is a mixture of variant and wild type TTR and no pure preparation of the variant has been available. For this reason, we constructed a system in which the variant type TTR was efficiently synthesized. In this system, the recombinant variant TTR was first synthesized as a fusion protein with E. coli outer membrane protein A (ompA) signal peptide, processed to eliminate the signal peptide and finally secreted to the culture medium. The final concentration of the recombinant variant TTR in the medium was about 5 mg/l. SDS polyacrylamide gel electrophoresis and gel filtration analysis suggested that the recombinant variant TTR can form tetramer as seen for native one. Purification of the protein was accomplished by only two steps of chromatography.

本文言語英語
ページ(範囲)851-859
ページ数9
ジャーナルBiochemical and Biophysical Research Communications
163
2
DOI
出版ステータス出版済み - 9 15 1989

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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