Abstract
Galactose- and inositol-binding proteins with lectin activity (GL-GAL and GL-I, respectively) were isolated from membranes enriched with cells of chicken brain fractions. Both lectins are glycoproteins of molecular mass 13.5 and 11.5 kDa, respectively; they show a high affinity to EDTA (GL-I) and EGTA (GL-GAL, GL-I), which indicates an important role of Ca+2 in molecular organization of these lectins. In brain glial cells of chick embryos, unlike adult chickens, a soluble form of lectins has been revealed; it is easily extracted with 2 mM EDTA and shows sensitivity to L-lactose, D-galactose, and N-acetyl-D-galactosamine. It is suggested that in the course of embryonal and postembryonal development of the chicken brain, a transformation and qualitative changes of the lectin spectrum occur due to a change of function of glial cells.
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Koshoridze, N.I., Aleksidze, N.G. & Surguladze, N.B. Inositol- and Galactose-Binding Lectins of Chicken Brain Fractions Enriched with Glial Cells. Journal of Evolutionary Biochemistry and Physiology 39, 446–450 (2003). https://doi.org/10.1023/B:JOEY.0000010241.34109.da
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DOI: https://doi.org/10.1023/B:JOEY.0000010241.34109.da