| Autor: |
Piskarev, V. E., Preisel, O. Yu., Evstigneeva, R. P., Yamskov, I. A. |
| Předmět: |
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| Zdroj: |
Applied Biochemistry & Microbiology; Jan/Feb2003, Vol. 39 Issue 1, p94-98, 5p |
| Abstrakt: |
The specificity of perch (Perca fluviatilis) roe fucolectin was studied using the protein dot blot technique, followed by detection with colloidal gold–labeled neoglycoproteins bearing human milk oligosaccharides. The strongest binding was noted with the H type 1 pentasaccharide lacto-N-fucopentaose (Fucα1-2Galβ1-3GlcNAcβ1-3Galβ1-4Glc); the interaction with the H type 6 trisaccharide 2"-fucosyllactose (Fucα1-2Galβ1-4Glc) was weaker. Binding of the perch lectin to the Lewis antigens (associated with tumors and embryonic tissues) was also studied. It was found that the lectin weakly interacted with the hexasaccharide lacto-N-difucohexaose I, Leb (Fucα1-2Galβ1-3[Fucα1-4]GlcNAcβ1-3Galβ1-4Glc), but not with Lea, Lec, or Lex antigens. Thus, the perch roe lectin exhibited pronounced differences in carbohydrate specificity from other fucolectins—a feature that may be used in structural studies and isolation of fucose-containing glycoconjugates. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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