Expression of human tyrosine hydroxylase type I in Escherichia coli as a protease-cleavable fusion protein

A. Nakashima, K. Mori, T. Nagatsu, A. Ota

研究成果: Article査読

10 被引用数 (Scopus)

抄録

Wild-type and N-terminal 35-, 38-, and 44-amino acid-deleted mutants of human tyrosine hydroxylase type 1 (hTH1) fused to maltose-binding protein via the target sequence for a restriction protease were expressed in Escherichia coli and purified. The fused protein was treated with the restriction protease factor Xa or enterokinase to isolate hTH1 from the fused form. The treatment of fused wild-type and 35-amino acid-deleted mutant with factor Xa and enterokinase caused non-specific cleavages in the vicinity of the phosphorylation sites, Ser19 and Ser40, due to the flexible conformation of the N-terminus of hTH1.

本文言語English
ページ(範囲)819-824
ページ数6
ジャーナルJournal of Neural Transmission
106
9-10
DOI
出版ステータスPublished - 1999

All Science Journal Classification (ASJC) codes

  • 神経学
  • 臨床神経学
  • 精神医学および精神衛生
  • 生物学的精神医学

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