Thiol-dependent Gelation of Conalbumin in the Presence of Denaturant(Food & Nutrition)
スポンサーリンク
概要
- 論文の詳細を見る
The effects of urea concentration on the dithiothreitol-dependent gelation of conalbumin (ovotransferrin) were investigated. In the presence of a high concentration of urea, conalbumin gelation was induced at lower molar ratios of dithiothreitol to protein than in the absence of the presence, but not in the absence of urea, intermolecular disulfide bonds were mainly involved in the gelation process. Under a scanning electron microscope, the gel formed in the presence of urea was composed of more fibrous networks than that formed in the absence of the denaturant.
- 社団法人日本農芸化学会の論文
- 1988-10-23
著者
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Doi Etsushiro
The Research Institute For Food Science Kyoto Univesity
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Hirose M
The Research Institute For Food Science Kyoto Univesity
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Doi Etsushiro
The Research Institute For Food Science Kyoto University
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Hirose Masaaki
The Research Institute For Food Science Kyoto Univesity
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OE Hideo
The Research Institute for Food Science, Kyoto University
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NISHIZAWA Yuriko
The Research Institute fo Food Science, Kyoto University
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Nishizawa Yuriko
The Research Institute Fo Food Science Kyoto University
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Hirose Masaaki
The Research Institute For Food Science Kyoto University
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Oe Hideo
The Research Institute For Food Science Kyoto University:(present Address)shiga Junior College Of Cu
関連論文
- Structural Characteristics of the Disulfide-reduced Ovotransferrin N-Lobe Analyzed by Protein Fragmentation
- Refolding of Urea-Denatured Ovalbumin That Comprises Non-Native Disulfide Isomers
- Role of the Intrachain Disulfide Bond of Ovalbumin during Conversion into S-Ovalbumin
- Periplasmic Secretion of Functional Ovotransferrin N-Lobe in Escherichia coli
- Structural Properties of Recombinant Ovalbumin and Its Transformation into a Thermostabilized Form by Alkaline Treatment
- Physicochemical and Functional Properties of Hen Ovalbumin Dephosphorylated by Acid Phosphatase(Food & Nutrition)
- Thiol-dependent Gelation of Conalbumin in the Presence of Denaturant(Food & Nutrition)
- Thiol-dependent Gelation of Conalbumin: Use of Thiosalicylic Acid and Its Removal from the Gel(Food & Nutrition)
- Effects of Anions on the Thiol-dependent Gelation of Conalbumin(Food & Nutrition)
- Conformation Changes and Subsequent Gelation of Conalbumin by a Thiol Reagent(Biological Chemistry)
- Subunit Structure of Sesame 13S Globulin
- Limited Proteolysis of Disulfide-reduced Ovalbumin by Subtilisin
- Conformational State of Disulfide-Reduced Ovalbumin at Acidic pH
- Involvement of Ovotransferrin in the Thermally Induced Gelation of Egg White at around 65℃
- Thiol-dependent Gelation of the Domain I-truncated Fragment of Bovine Serum Albumin
- Highly Ordered Molten Globule-Like State of Ovalbumin at Acidic pH: Native-Like Fragmentation by Protease and Selective Modification of Cys367 with Dithiodipyridine
- The Structural Mechanism for Iron Uptake and Release by Transferrins
- Roles of the Domain I Segment in Emulsifying Properties of Bovine Serum Albumin
- Properties of Ovalbumin Limited-proteolyzed by Pepsin on Heating(Food & Nutrition)
- Purification and Characterization of Rice Embryo BAPAase (Benzoyl-L-arginine p-nitroanilide Hydrolase)
- A Novel Type of Substrate Specificity of Rice BAPAase (Benzoyl-L-atginine p-nitroanilide Hydrolase) with Mixed Endopeptidase and Carboxypeptidase