| Autor: |
Kawsar, S. M. A., Matsumoto, R., Fujii, Y., Yasumitsu, H., Dogasaki, C., Hosono, M., Nitta, K., Hamako, J., Matsui, T., Kojima, N., Ozeki, Y. |
| Předmět: |
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| Zdroj: |
Biochemistry (00062979); Jul2009, Vol. 74 Issue 7, p709-716, 8p, 3 Charts, 5 Graphs |
| Abstrakt: |
A lectin was purified from Japanese sea hare Aplysia kurodai by lactosyl-agarose affinity chromatography. The molecular mass of the lectin was determined to be 56 and 32 kDa by SDS-PAGE under non-reducing and reducing conditions, respectively. It was found to agglutinate trypsinized and glutaraldehyde-fixed rabbit and human erythrocytes in the absence of divalent cations. The lectin exhibited stable thermo-tolerance as it retained hemagglutinating activity for 1 h even at 80°C and showed stability at pH 10. By contrast, it was very sensitive at pH less than 5 and in the presence of the sulfhydryl-group preserving reagent, β-mercaptoethanol. The hemagglutinating activity by the lectin was specifically inhibited by D-galactose, galacturonic acid, methyl-α- and methyl-β-D-galactopyranoside, lactose, melibiose, and asialofetuin. The association rate constant ( kass) and dissociation rate constant ( kdiss) were determined for the lectin to be 4.3·105 M−1·sec−1 and 2.2·10−3 sec−1, respectively, using a surface plasmon resonance biosensor. The lectin moderately inhibited cell proliferation in the P388 cell line dose dependently. Interestingly, lectin-treated cells did not show a fragmented DNA ladder as is caused by apoptosis, suggesting that the cell proliferation inhibition was caused by another unknown mechanism. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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