Purification and Partial Characterization of an Acidic α-Glucan–Protein Complex from the Fruiting Body of Pleurotus sajor-caju and Its Effect on Macrophage Activation
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- SATITMANWIWAT Saranya
- School of Bioresources and Technology, King Mongkut's University of Technology Thonburi School of Bioresources and Technology, King Mongkut's University of Technology Thonburi
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- RATANAKHANOKCHAI Khanok
- School of Bioresources and Technology, King Mongkut's University of Technology Thonburi School of Bioresources and Technology, King Mongkut's University of Technology Thonburi
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- LAOHAKUNJIT Natta
- School of Bioresources and Technology, King Mongkut's University of Technology Thonburi School of Bioresources and Technology, King Mongkut's University of Technology Thonburi
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- PASON Patthra
- Pilot Plant Development and Training Institute, King Mongkut's University of Technology Thonburi Pilot Plant Development and Training Institute, King Mongkut's University of Technology Thonburi
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- TACHAAPAIKOON Chakrit
- Pilot Plant Development and Training Institute, King Mongkut's University of Technology Thonburi Pilot Plant Development and Training Institute, King Mongkut's University of Technology Thonburi
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- KYU Khin Lay
- School of Bioresources and Technology, King Mongkut's University of Technology Thonburi School of Bioresources and Technology, King Mongkut's University of Technology Thonburi
書誌事項
- タイトル別名
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- Purification and Partial Characterization of an Acidic α-Glucan–Protein Complex from the Fruiting Body of <i>Pleurotus sajor-caju</i> and Its Effect on Macrophage Activation
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The aim of this study was to purify an acidic α-glucan–protein complex from the fruiting bodies of Pleurotus sajor-caju by using the cell wall-degrading enzymes, xylanase and cellulase. The acidic glucan–protein complex was separated from a polysaccharide extract by using DEAE Toyopearl 650M anion-exchange and Sepharose CL-6B chromatography. Its homogeneity was ensured by high-performance size-exclusion chromatography and agarose gel electrophoresis. The acidic glucan–protein complex had a molecular weight of approximately 182 kDa. Fourier transform infrared spectroscopy of the acidic glucan–protein complex revealed an α-glycosidic bond and the typical characteristics of polysaccharides and proteins. The amino acid composition of the protein moiety was dominated by proline, glycine, glutamic acid and aspartic acid, indicating that the protein was highly flexible and had a negative charge. Atomic force microscopy proved that the acidic α-glucan–protein complex existed in a spherical conformation. The acidic α-glucan–protein complex stimulated the activation of macrophages, including the production of nitric oxide and tumor necrosis factor-α.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 76 (10), 1884-1890, 2012
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206478358400
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- NII論文ID
- 130004054005
- 10031126475
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- NII書誌ID
- AA10824164
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- COI
- 1:STN:280:DC%2BC3s%2FjsFGmsA%3D%3D
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 024035905
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- PubMed
- 23047100
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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