Liberation of Subunit Polypeptides of Glutenin by Partial Reduction at pH 6.0
スポンサーリンク
概要
- 論文の詳細を見る
Glutenin was reduced with various concentrations of 2-mercaptoethanol (2-ME) at pH 6.0 and the liberation of subunits was observed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The amount of sulfhydryl groups in protein (protein-SH) liberated by reduction increased steeply with the increase of 2-MEconcentration around 1 mM.But the increase of protein-SH declined at higher concentrations to give a plateau at 6 mM.The level of this plateau, which may correspond to the amount of reactive disulfide (SS) bonds, was 40%of the total SS bonds of glutenin. In order to investigate whether inter-polypeptide SS bonds are cleaved by the partial reduction, the liberation of subunit monomers was observed by SDS-PAGE.By the partial reduction, Band 1+1′ (MW 104Kd), Band 2 (MW 90 Kd), Band 3 (MW 81 Kd) and Band 7 (MW 35 Kd) appeared in the electrophoretic pattern even at low concentrations of 2-ME, indicating the liberation of these subunits. However, although all monomersof Band 7 subunits were almost liberated at low concentrations of 2-ME (0.5mM), Bands 1+1′, 2, and 3 did not show suffic ient amounts of monomerseven at 6 mM.Further, another group of band, which had molecular weights of 136 Kd, 132 Kd, and 1 10 Kd, were observed at low concentrations of2-ME but dissapeared at extremely high concentrations, indicating these bands must be oligomers of glutenin subunits. These observations from the SDS-PAGE patterns suggested that the reactivities of interpolypeptide SS bonds differ according to the kinds ofsubunits. Band 6 (MW42 Kd) appeared at the position of MW38 Kd by reduction with lower concentrations of2-ME, indicating the retention of intra-polypeptide SS bonds. Bands 1+1′ 2, 3, and 7 that always appeared at the same positions independent of the 2-MEconcentrations, were separated from partial reduced glutenin (0.5 mMof 2-ME) and their SHand SS determined, in order to knowwhether these subunits retain intrapo lypeptide SS bonds. While the amount of liberated SH was much less than 2 mol per mol protein, the amount of SS bands was near 2mol, indicating that the liberated subunits retain intrapolypeptide SS bonds.
- 社団法人 日本農芸化学会の論文
著者
-
Matoba Teruyoshi
Research Institute For Food Science Kyoto University
-
Matsumura Yasuki
Research Institute For Food Science Kyoto University
-
KAWAMURA Yukio
Research Institute for Food Science, Kyoto University
-
YONEZAWA Daizo
Faculty of Domestic Science, Mukogawa Womens University
関連論文
- Effects of Deamidation and Fragmentation on Antioxidative Activity of α-Zein
- Gelation of Bean 11S Globulins by Ca^ -Independent Transglutaminase
- Separation of Subunit Polypeptides of Glutenin by SDS-PAGE and Determination of Their Cysteine Contents
- Lysosomal nature of plant vacuoles II. Acid hydrolases in the central vacuole of internodal cells of Charophyta
- Lysosomal nature of plant vacuoles I. Apparent absence of lysosomal particles in tomato fruit and leaf homogenates
- Effects of Carnauba Wax Addition on Physical States of Palm Kernel Oil-in-Water Emulsions
- Conformational Changes and Surface Properties of Legumin from Broad Beans in Relation to Its Thermal Aggregation
- Relationships of Molecular Forces to Rheological and Structural Properties of Legumin Gels from Broad Beans
- Relationship between the Thermal Denaturation and Gelling Properties of Legumin from Broad Beans
- Effects of Fragmentation and Deamidation on the Antioxidative Activity of C Hordein
- Interaction of Gum Arabic, Maltodextrin and Pullulan with Lipids in Emulsions
- Effects of Fragmentation and Deamidation on the Antioxidative Activity of C Hordein.
- Liberation of Subunit Polypeptides of Glutenin by Partial Reduction at pH 6.0
- Changes in Casein and Egg Albumin due to Reactions with Oxidizing Methyl Linoleate in Dehydrated Systems
- Characteristics of Autolysis of Antarctic Krill
- Wheat Flour Proteases and Their Action on Gluten Proteins in Dilute Acetic Acid
- Deterioration of Antarctic Krill Muscle during Freeze Storage
- Effects of Protease Inhibitors on the Autolysis and Protease Activities of Antartic Krill
- In Vitro Enzymatic Determination of the Protein Nutritional Value and the Amount of Available Lysine in Extruded Cereal-based Products
- An Approach to Assessing the Gastro-intestinal Digestion of Rice and Wheat Proteins: Use of a Model System with Pepsin, Pancreatin and Intracellular Peptidases
- Changes in Molecular Size and Chemical Properties of Gelatin Caused by the Reaction with Oxidizing Methyl Linoleate