Purification and characterization of lectin from humoral fluids of Charybdis feriatus
To search new sources of lectin, an experiment on lectin distribution in humoral serum of crab Charybdisferiatus (in short, CFL) was conducted March, 2002. When adding solid ammonium sulfate into the fluids up to 50% saturation at 4℃, most CFL activity showed precipitates who were then continually e...
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Published in | Chinese journal of oceanology and limnology Vol. 24; no. 4; pp. 390 - 394 |
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Main Author | |
Format | Journal Article |
Language | English |
Published |
Department of Oceanography, State key Lab of Marine Environmental Sciences, Xiamen University, Xiamen 361005, China
2006
Department of Biology Quanzhou Normal College, Quanzhou 362000, China%Department of Oceanography, State key Lab of Marine Environmental Sciences, Xiamen University, Xiamen 361005, China%Polar Research Institute of China, Shanghai 200136, China Polar Research Institute of China, Shanghai 200136, China |
Subjects | |
Online Access | Get full text |
ISSN | 0254-4059 |
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Summary: | To search new sources of lectin, an experiment on lectin distribution in humoral serum of crab Charybdisferiatus (in short, CFL) was conducted March, 2002. When adding solid ammonium sulfate into the fluids up to 50% saturation at 4℃, most CFL activity showed precipitates who were then continually extracted by ammonium sulfate of different concentrations. The supernatant, which was called primary CFL fluids, was given a 17.60-fold purification and 45.70% recovery of total activity. Finally, by using Sephadex G-100 column chromatography, the CFL in the primary CFL fluid was highly purified, Compared to the original humoral fluids, the last purified CFL got a 203.90-fold purification and 30.48% recovery of total activity, and demonstrated a single band on SDS-PAGE. In the same time, the purified CFL was detected for agglutination activity with 7 kinds of animal erythrocytes. Other characterization, such as sugar inhibition, and the effect of temperature on the agglutination activity of CFL were also studied. Our results indicate that agglutination activity of CFL was influenced by sugar and temperature. |
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Bibliography: | CFL (lectin from Charybdisferiatus) ammonium sulfate purification 37-1150/P ammonium sulfate; purification; CFL (lectin from Charybdisferiatus); characterization characterization P734.2 |
ISSN: | 0254-4059 |