Thiol-dependent Gelation of Conalbumin: Use of Thiosalicylic Acid and Its Removal from the Gel(Food & Nutrition)
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概要
- 論文の詳細を見る
- 社団法人日本農芸化学会の論文
- 1988-01-23
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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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