Abstract:This study sought to have an insight into the mechanism of action of diseases responsible for the susceptible Codiaeum variegatum (garden croton) leaves induced by Fusarium species and the clinical importance of the d isease resistant types. The plants were obtained fro m the Babcock University Germp lasm Repository. Therefore, phytopathogenic Fusarium species were isolated fro m three diseased susceptible cult ivars of C. variegatum (ovalifolium, royal-like and punctatum). Accordingly, lect in was isolated, p… Show more
“…This is slightly similar to the lectin extracted from Codiaeum variegatum [29]. Lectin in this study was found to be heat stable from 20˚C to 30˚C and the heat stability began to decrease at 40˚C and completely lost its activity at 70˚C.…”
Section: Discussionsupporting
confidence: 80%
“…As shown in the result virtually all the lectins from the various strains of Schizophyllum commune are Mannose binding. This type of lectin is quite different from the recently reported Lectin [29]. As known they have attracted great interest due to their various biological activities, such as antitumor [30] [31].…”
Haemagglutination studies on lectin from both wild (SCW) and mutant strains (SCM1, SCM2, SCM3) of Schizophyllum commune using human blood were explored in this study after six days of submerged fermentation. Haemagglutination assay showed that the lectin from all the strains showed slight discrimination in their haemmaglutinating activity against human blood group with strong exhibition of agglutination with blood group O while SCM3 and SCW showed the highest and lowest haemaglutinating activity respectively with a titre score from 4 -256 HA. Absolute loss of haemagglutination activity was shown by all the four S. commune strains tested following exposure to CuSO4 and NH 4 SO 4 at 800 mM but optimized by KCl, MgCl 2 at 100 mM. Optimal pH for maximal haemagglutination activity was observed at 7.0 for SCW, 6.0 for SCM1 and 8.0 for SCM2 while SCM3 distinctly showed 5.5 and 8.5. Except for SCM3 the thermo stability of haemagglutinating activity was found to improve with the duration of UV irradiation. Inhibitory study in the presence of sugar showed that the partially purified protein from all the strains of S. commune in this study was mannose dependent lectin.
“…This is slightly similar to the lectin extracted from Codiaeum variegatum [29]. Lectin in this study was found to be heat stable from 20˚C to 30˚C and the heat stability began to decrease at 40˚C and completely lost its activity at 70˚C.…”
Section: Discussionsupporting
confidence: 80%
“…As shown in the result virtually all the lectins from the various strains of Schizophyllum commune are Mannose binding. This type of lectin is quite different from the recently reported Lectin [29]. As known they have attracted great interest due to their various biological activities, such as antitumor [30] [31].…”
Haemagglutination studies on lectin from both wild (SCW) and mutant strains (SCM1, SCM2, SCM3) of Schizophyllum commune using human blood were explored in this study after six days of submerged fermentation. Haemagglutination assay showed that the lectin from all the strains showed slight discrimination in their haemmaglutinating activity against human blood group with strong exhibition of agglutination with blood group O while SCM3 and SCW showed the highest and lowest haemaglutinating activity respectively with a titre score from 4 -256 HA. Absolute loss of haemagglutination activity was shown by all the four S. commune strains tested following exposure to CuSO4 and NH 4 SO 4 at 800 mM but optimized by KCl, MgCl 2 at 100 mM. Optimal pH for maximal haemagglutination activity was observed at 7.0 for SCW, 6.0 for SCM1 and 8.0 for SCM2 while SCM3 distinctly showed 5.5 and 8.5. Except for SCM3 the thermo stability of haemagglutinating activity was found to improve with the duration of UV irradiation. Inhibitory study in the presence of sugar showed that the partially purified protein from all the strains of S. commune in this study was mannose dependent lectin.
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