Study on Determination of Hegglutination Ativity of the Lectin from Canavalia ensiformis(L.) DC and its Characteristics
Jingyi Chen
Abstract
Jingyi Chen
Abstract
[Objective] The aim of this research was to provide the base for studying the lectin from Canavalia ensiformis(L.) DC.[Method] The concanavalin A(ConA)was extracted from the dry mature seed of C.ensiformis(L.) DC,its hegglutination activity was determined and its part characteristics were studied.[Result] It as found the agglutinative activity of ConA could increase 8 times when detected with human red cell treated by typsin.ConA can agglutinate A、B、O and AB types of human blood and the erythrocytes of rabbit, chicken,duck,pigeon,common carp and crucian carp,without sepicificity of erythocyte agglutination.D-Glucose and D-Mannose were just the sugar which could band ConA specifically.ConA was a kind of lectin stable to heat treatment.It was stable at below 40 ℃,but it was completely inactive at above 80 ℃ for 20 min.ConA had higher lectin activity at pH of 5.8~8.3,but its lectin activity was inactive at pH above 11.9.The lectin activity of ConA was completely inactive when the denaturant urea concentration reached over 4 mol/L.[Conclusion] This study has important meaning for clarifying the biology function of ConA systematically in future and enlarging its application range.
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[Objective] The aim of this research was to provide the base for studying the lectin from Canavalia ensiformis(L.) DC.[Method] The concanavalin A(ConA)was extracted from the dry mature seed of C.ensiformis(L.) DC,its hegglutination activity was determined and its part characteristics were studied.[Result] It as found the agglutinative activity of ConA could increase 8 times when detected with human red cell treated by typsin.ConA can agglutinate A、B、O and AB types of human blood and the erythrocytes of rabbit, chicken,duck,pigeon,common carp and crucian carp,without sepicificity of erythocyte agglutination.D-Glucose and D-Mannose were just the sugar which could band ConA specifically.ConA was a kind of lectin stable to heat treatment.It was stable at below 40 ℃,but it was completely inactive at above 80 ℃ for 20 min.ConA had higher lectin activity at pH of 5.8~8.3,but its lectin activity was inactive at pH above 11.9.The lectin activity of ConA was completely inactive when the denaturant urea concentration reached over 4 mol/L.[Conclusion] This study has important meaning for clarifying the biology function of ConA systematically in future and enlarging its application range.
Key concepts: Canavalia ensiformis, Concanavalin A, Lectin, Agglutination (biology), Agglutinin, Biology, Crucian carp, Hemagglutination