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- HASHIMOTO Yoshio
- Graduate School of Pharmaceutical Sciences, Kyushu University
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- MUNEMURA Osamu
- Graduate School of Pharmaceutical Sciences, Kyushu University
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- MASUMOTO Kiyonari
- Graduate School of Pharmaceutical Sciences, Kyushu University
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- UEDA Tadashi
- Graduate School of Pharmaceutical Sciences, Kyushu University
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- IMOTO Taiji
- Graduate School of Pharmaceutical Sciences, Kyushu University
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抄録
We prepared a lysozyme mutant (Q41S/R61S) introducing Asn-type glycosylation signal sites by yeast expression system. On purification by cation exchange column at pH 7, three fractions were obtained. Peptide mapping and mass-spectrometry showed the fractions were the derivatives glycosylated at both Asn39 and Asn59, at only Asn39, and not glycosylated. It was revealed that the processing of Asn-linked oligosaccharide at Asn39 and Asn59 occurred independently in yeast cells. The denaturation temperatures of these derivatives by differential scanning calorimetry were 76.0, 68.8, and 67.5°C at pH 3, respectively. The stabilization of glycosylated lysozyme depends on the degree of glycosylation. We concluded that stabilized proteins can be constructed by glycosylation at proper sites. Thermodynamic stabilization by the artificial double glycosylations on a protein has not yet been reported.
収録刊行物
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- Biological & Pharmaceutical Bulletin
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Biological & Pharmaceutical Bulletin 24 (10), 1102-1107, 2001
公益社団法人 日本薬学会
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詳細情報 詳細情報について
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- CRID
- 1390001204624726272
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- NII論文ID
- 110003638364
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- NII書誌ID
- AA10885497
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- COI
- 1:CAS:528:DC%2BD3MXnt12jtLs%3D
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- ISSN
- 13475215
- 09186158
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- NDL書誌ID
- 5926460
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- PubMed
- 11642311
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可