Improvement of the refolding yield and solubility of hen egg-white lysozyme by altering the Met residue attached to its N-terminus to Ser

Shouhei Mine, Tadashi Ueda, Yoshio Hashimoto, Taiji Imoto

研究成果: Contribution to journalArticle査読

35 被引用数 (Scopus)

抄録

When hen egg-white lysozyme was produced in Escherichia coli, it possessed an extra methionine residue at the N-terminus (Met-1-lysozyme). The Met-1-lysozyme showed a decreased refolding yield and solubility compared with the native hen egg-white lysozyme, as the methionine is a hydrophobic amino acid. A Met-2Pro-1 or Met-2Ser-1 sequence was introduced at the N-terminus of hen egg-white lysozyme. The methionine residue in these hen egg-white lysozymes was completely removed by methionine aminopeptidase, as expected, since the penultimate residue was proline or serine. From the analyses of solubility, stability and refolding yield, it was found that an extra Ser residue attached to the N-terminus of hen egg-white lysozyme (Ser-1-lysozyme) showed closer characteristics to the native hen egg-white lysozyme than did Met-1 or an extra Pro residue attached to the N-terminus of hen egg-white lysozyme (Pro-1-lysozyme). Moreover, the tertiary conformation of Ser-1-lysozyme examined by NMR spectroscopy and its activity were almost identical with those of native hen egg-white lysozyme.

本文言語英語
ページ(範囲)1333-1338
ページ数6
ジャーナルProtein Engineering
10
11
DOI
出版ステータス出版済み - 1997

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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