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1

Fasciola hepatica miracidia: Lectin binding and stimulation of in vitro miracidium-to-sporocyst transformation

100%
Georgieva K., Georgieva S., Mizinska Y., Stoitsova S. R.
Acta Parasitologica
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2012
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tom 57
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nr 1
The lectin binding properties of Fasciola hepatica miracidia were studied by a panel of fluorescein- and gold-conjugated lectins (ConA, LCA, WGA, LEA, SBA, HPA and UEA-I). The presence of mannose and/or glucose residues was demonstrated with ConA and LCA as weak diffuse fluorescence of the miracidial surface, which was more intense at the anterior part of the larva. The N-acetylglucosamine-binding lectins WGA and LEA reacted intensely with the whole miracidial surface. No labelling with N-acetylgalactosamine and/or galactose-specific (SBA and HPA) and fucose-specific UEA-I lectins was observed. The possibility that the specific recognition of the miracidial surface carbohydrates by lectins may initiate the process of transformation of the miracidia into sporocysts was examined in vitro in physiological saline for Galba truncatula. Incubation in the presence of ConA and WGA resulted in facilitation of the transformation process. Facilitation was absent in the presence of inhibitor sugars. Incubation in the presence of SBA or UEA-I had no effect. The results suggested a possible impact of carbohydrate-lectin interactions in transformation of miracidia of F. hepatica to sporocysts in vivo.
2

Isoenzymes of N-acetyl-beta-hexosaminidase

100%
Zwierz K., Zalewska A., Zoch-Zwierz W.
Acta Biochimica Polonica
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1999
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tom 46
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nr 3
Biological significance, structure and posttranslational processing of N-acetyl-β-hexosaminidase isoenzymes are described. Clinical application of N-acetyl-β-hexosaminidase is also reviewed.
3

Glycophorin A in two patients with congenital dyserythropoietic anemia type I and type II is partly unglycosylated

100%
Zdebska E., Adamczyk-Poplawska M., Koscielak J.
Acta Biochimica Polonica
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2000
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tom 47
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nr 3
Glycophorins A from erythrocyte membranes of two patients with congenital dyserythropoietic anemia type I and type II (CDA type I and II) were analyzed for carbohydrate molar composition employing a modification of the recently published method that allowed simultaneous determination of carbohydrates and protein in electrophoretic bands of glycoproteins separated by sodium dodecyl sulfate- polyacrylamide gel electrophoresis (Zdebska & Koscielak, 1999, Anal. Biochem., 275, 171-179). The modification involved a preliminary extraction of erythrocyte membranes with aqueous phenol, subsequent electrophoresis and analysis of the extracted glycophorins rather than electrophoresis and analysis of the glycophorin from intact erythrocyte membranes. The results showed a large deficit of N-acetylgalactosamine, galactose, and sialic acid residues in glycophorin A from patients with CDA type I and type II amounting to about 45% and 55 %, respectively. The results strongly suggest that glycophorin A in these patients is partly unglycosylated with respect to O-linked glycans. In addition, glycophorin A from erythrocytes of a patient with CDA II but not CDA I exhibited a significant deficit of mannose and N-acetylglucosamine suggesting that its N-glycosylation site was also partly unglycosylated.
4

Similarity of vitamin D-binding protein (DBP) between various animal species in double immunodiffusion and western blotting

80%
Madej J. P., Boratynski J., Nowacki W.
Electronic Journal of Polish Agricultural Universities. Series Veterinary Medicine
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2007
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tom 10
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nr 3
5

The N-acetylgalactosamine and lactosamine specific lectin from Iris hybrida leaves

80%
Ferens-Sieczkowska M., Orczyk-Pawilowicz M., Morawiecka B.
Acta Biochimica Polonica
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1997
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tom 44
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nr 2
The lectin isolated from the leaves of Iris hybrida binds specifically N-acetyl-galactosamine and lactose. Its molecule consists of two identical subunits bound by disulfide bonds. The lectin is a glycoprotein containing about 12% of sugars. It binds asialoglycoproteins containing complex type sugar chains. The binding is reduced by half at the concentration of 0.15 to 0.40 mM of the galactose containing disaccharides irrespectively to a type of galactose isomer. This indicates rather broad specificity of I. hybrida leaf lectin.
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