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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.
2
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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
3
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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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4
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Molecular analysis of three novel G6PD variants: G6PD Pedoplis-Ckaro, G6PD Piotrkow and G6PD Krakow

64%
Maciag M., Plochocka D., Jablonska-Skwiecinska E., Mendek-Czajkowska E., Golaszewska E., Strojny W., Balwierz W., Zdebska E., Burzynska B.
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2007
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vol. 54
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issue 4
877-881
EN
We present three novel mutations in the G6PD gene and discuss the changes they cause in the 3-dimensional structure of the enzyme: 573C→G substitution that predicts Phe to Leu at position 191 in the C-terminus of helix αe, 851T→C mutation which results in the substitution 284Val→→Ala in the β+α domain close to the C-terminal part of helix αj, and 1175T→C substitution that predicts Ile to Thr change at position 392.
5
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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
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