期刊
APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
卷 172, 期 4, 页码 2081-2090出版社
HUMANA PRESS INC
DOI: 10.1007/s12010-013-0665-5
关键词
Lectin; Gymnopilus spectabilis; Basidiomycete; Fruiting body; Glycoproteins
资金
- Comision Sectorial de Investigacion Cientifica (Universidad de la Republica, Uruguay) [325]
- Program for Technological Development Project [74-12]
- Program for the Development of Basic Sciences (PEDECIBA-Quimica)
- Agencia Nacional de Investigacion e Innovacion, Uruguay
A lectin was isolated from fruiting bodies of the mushroom Gymnopilus spectabilis (GSL) by ionic exchange chromatography. The lectin agglutinates mouse red cells exhibiting broad specificity towards several monosaccharides including the N-acetylneuraminic acid. Agglutination was also inhibited by the glycoproteins: fetuin, lactoferrin, and recombinant erythropoietin. GSL is a glycoprotein possessing 16 % of carbohydrates; the SDS-PAGE showed two bands with molecular mass of 52.1 and 64.4 kDa. Isoelectric focusing displayed microheterogeneity, with two bands at pIs 5.1 and 5.3. The lectin was stable between pH 2 and pH 8 while at pH 10, the agglutination decayed to 50% of initial activity. Incubation at 40 and 80 degrees C led to 50 and 100 % loss in activity of the lectin, respectively. Synthesized GSL-Sepharose interacts with serum pregnant mare gonadotropin, and at least two subpopulations of this glycoprotein were separated. There was no interaction between transferrin and soluble GSL while a partial recognition was achieved with GSL-Sepharose. The terminal sialic acid seems to play an active role in modifying the interaction with GSL, depending if the lectin is in a soluble or immobilized form. The purified lectin inhibited in vitro the growth of Staphylococcus aureus and Aspergillus niger.
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