碩士 / 國立臺灣大學 / 農業化學研究所 / 90 / Agglutinins have been isolated and characterized from various biological sources. Agglutinins are proteins with carbohydrate-binding sites which have the ability to agglutinate erythrocytes. In the present study, 17 strains of Chlorella species was analyzed for hemagglutinating activity using human erythrocytes A, B, O and AB groups, in addition to those of pig, cow, goat. A new agglutinin was isolated from C. luteoviridis by using a purification procedure that comprised physiological saline extration, DEAE-C-52 ion exchange chromatography, CM-C-52 ion exchange chromatography, and Superdex 75 gel filtration. The hemagglutinating activity was detected for almost Chlorella species. The results suggest the use of different types of erythrocytes for detection of agglutinins in algal extracts even when the erythrocytes are enzyme-treated. Chlorella species assayed displayed strong affinity toward B erythrocytes. C. luteoviridis agglutinin is a single protein and its molecular mass of 83 kDa. For elucidating the properties of C. luteoviridis agglutinin, we examined C. luteoviridis agglutinin for agglutinating activities toward erythrocytes, it has a wide range of pH and temperature of agglutination. Agglutinating activities were strongly inhibited by glycoproteins such as Mucin, Asialofetuin, but not by monosaccharides (D-Glucose, D-Mannose, D-Glucose, L-Fucose), suggesting that C. luteoviridis agglutinin binds specifically to some complex carbohydrates.
Identifer | oai:union.ndltd.org:TW/090NTU00406008 |
Date | January 2002 |
Creators | Shi-Li Chen, 陳旭麗 |
Contributors | Liang-Ping Lin, Liao-Woan Ru, 林良平, 廖婉茹 |
Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
Language | zh-TW |
Detected Language | English |
Type | 學位論文 ; thesis |
Format | 70 |
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