Fractionation of kintoki bean lectin into isolectins.
スポンサーリンク
概要
- 論文の詳細を見る
A comprehensive study of the preparative procedure of Kintoki bean lectin resulted in the resolution of the lectin into four Isolectins whose pIs varied from 5.19 to 5.67. They agglutinated human, goat, hen and mouse erythrocytes, but not those of cow. The more acidic the isolectins, the less active were the erythrocyte agglutination and the more active the stimulation of sheep lymphocytes. Although the general patterns of amino acid composition were similar, characterized by higher contents of aspartic acid, leucine and valine and lack of sulfur-containing amino acids, differences were found in a few amino acids such as phenylalanine, valine and lysine. Each lectin seems to be a tetramer of a 33, 000 dalton subunit which is thought to differ in charge from lectin to lectin.
- 財団法人 学会誌刊行センターの論文
著者
-
塚本 幾代
Laboratory of Nutritional Chemistry, Department of Food Science and Nutrition, Nara Women's University
-
椋 容子
Laboratory of Nutritional Chemistry, Department of Food Science and Nutrition, Nara Women's University
-
三好 正満
Graduate Division of Human Culture, Nara Women's University
-
原 知子
Graduate Division of Human Culture, Nara Women's University
-
原 知子
Graduate Division of Human Culture, Nara Women's University
-
原 知子
Graduate Division of Human Culture (Doctoral Degree Program), Nara Women's University
関連論文
- Toxic Effects of Kintoki Bean (Phaseolus vulgaris) Lectin on Cultured Animal Cells
- The Lethal Protein from Kintoki Beans (Phaseolus vulgaris) Identified as a Lectin
- Fractionation of kintoki bean lectin into isolectins.
- The effect of lectin from taro tuber (Colocasia antiquorum) given by force-feeding on the growth of mice.
- Oral toxicity of Kintoki bean (Phaseolus vulgaris) lectin.