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1
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In comparison to progenitor platelets, microparticles are deficient in GpIb, GpIb-derived carbohydrates, glycerophospholipids, glycosphingolipids, and ceramides

100%
Zdebska E., Woźniak J., Dziecištkowska A., Kościelak J.
Acta Biochimica Polonica
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1998
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vol. 45
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issue 2
417-428
2
Content available remote

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

100%
Zdebska E., Adamczyk-Popławska M., Kościelak J.
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2000
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vol. 47
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issue 3
773-779
EN
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 & Kościelak, 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.
3
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The levels of glycosphingolipids, ceramides, sialic acid and glycogen are changed in plasma membranes of rat platelets harvested during recovery from immune-mediated thrombocytopenia

100%
Zdebska E., Soszyńska B., Dobrowolski Z., Kościelak J.
Acta Biochimica Polonica
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1996
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vol. 43
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issue 3
547-555
4
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Paul-Bunnell antigen and a possible mechanism of formation of heterophile antibodies in patients with infectious mononucleosis.

100%
Gołaszewska E., Kurowska E., Duk M., Kościelak J.
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2003
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vol. 50
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issue 4
1205-1211
EN
Sera of patients with infectious mononucleosis contain heterophile anti-Paul- Bunnell (PB) antibodies to erythrocytes of numerous mammalian species. Evidence is presented that the corresponding antigen of bovine erythrocytes is not, as previously described, a single molecule, but a series of glycoproteins with glycans terminated with N-glycolylneuraminic acid (Neu5Gc). The latter compound should be an important part of the PB epitope because, in agreement with the results of others, we found that desialylation of the PB antigen abolishes almost completely its activity. We examined three different preparations of GM3 ganglioside for their capacity to bind anti-PB and found that only GM3 from horse erythrocytes containing Neu5Gc exhibited a low although ELISA measurable PB activity. The other two GM3 preparations, from bovine milk and dog erythrocytes, containing N-acetylneuraminic acid (Neu5Ac) bound little if any anti-PB antibodies. This finding confirms a previous report that human erythrocyte Neu5Ac containing sialoglycoprotein with similar O-linked glycans as the PB-antigen of bovine erythrocytes exhibits only very low PB activity (Patarca & Fletcher, 1995, Crit Rev Oncogen., 6: 305). In conclusion, we present a hypothesis that anti-PB antibodies in patients with infectious mononucleosis are formed against infection-induced cell membrane glycoconjugates containing highly immunogenic Neu5Gc.
5
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Activity of platelet α-6-fucosy1transferase is inversely related to blood platelet concentration

88%
Kościelak J., Antoniewicz-Papis J., Zdebska E., Maj S., Leszko B.
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6
Content available remote

Contents of total and protein-bound carbohydrates are low in leukemic leukocytes from patients with acute myelogenous leukemia

64%
Smoleńska-Sym G., Zdebska E., Gołaszewska E., Woźniak J., Durżyński T., Maj S., Mokras U., Kościelak J.
Acta Biochimica Polonica
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1998
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vol. 45
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issue 2
361-371
7
Content available remote

Carbohydrate-deficient glycoprotein syndromes

62%
Kościelak J.
Acta Biochimica Polonica
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1999
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vol. 46
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issue 3
727-738
8
Content available remote

Diseases of aberrant glycosylation

50%
Kościelak J.
Acta Biochimica Polonica
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1995
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vol. 42
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issue 1
1-10
9
Content available remote

Book review

37%
Kościelak J.
Acta Biochimica Polonica
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1997
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vol. 44
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issue 2
365
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