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1

Molecular topography of a transmembrane protein: glycophorin A

100%
Nakatani Y., Hahn W., Garnier P., Higashi N., Ourisson G., Sunamoto J.
Cellular and Molecular Biology Letters
|
1999
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tom 04
|
nr 2
2

Interaction of glycophorin A with lectins as measured by surface plasmon resonance [SPR]

75%
Krotkiewska B., Pasek M., Krotkiewski H.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 2
Glycophorin A (GPA), the major sialoglycoprotein of the human erythrocyte mem­brane, was isolated from erythrocytes of healthy individuals of blood groups A, B and O using phenol-water extraction of erythrocyte membranes. Interaction of individual GPA samples with three lectins (Psathyrella velutina lectin, PVL; Triticum vulgaris lectin, WGA and Sambucus nigra I agglutinin SNA-I) was analyzed using a BIAcore™ biosensor equipped with a surface plasmon resonance (SPR) detector. The experi­ments showed no substantial differences in the interaction between native and desialylated GPA samples originating from erythrocytes of either blood group and each of the lectins. Desialylated samples reacted weaker than the native ones with all three lectins. PVL reacted about 50-fold more strongly than WGA which, similar to PVL, recognizes GlcNAc and Neu5Ac residues. SNA-I lectin, recognizing α2-6 linked Neu5Ac residues, showed relatively weak reaction with native and only residual reac­tion with desialylated GPA samples. The data obtained show that SPR is a valuable method to determine interaction of glycoproteins with lectins, which potentially can be used to detect differences in the carbohydrate moiety of individual glycoprotein samples.
3

Subtle differences in glycosylation of blood group M and N type glycophorin A detected with anti-Tn lectins and confirmed by chemical analysis

75%
Krotkiewski H., Duk M., Lisowska E.
Acta Biochimica Polonica
|
1995
|
tom 42
|
nr 1
A higher content of Tn and sialyl-Tn receptors in glycophorin A of blood group N than in that of blood group M was suggested by reactions with anti-Tn lectins. Analysis of [^-elimination products of two blood group M and two blood group N preparations by gas liquid chromatography-mass spectrometry showed that GalNAc- -ol was detectable in minor amounts in all analyzed samples and its content was higher in the products obtained from desialylated antigens. Moreover, the content of Gal N Ac- -ol detected in blood group N samples was almost twice as high as in respective blood group M samples. Since blood group M and N antigens differ in two amino-acid residues, our results support the existence of sequence-dependent differences in efficiency of substitution of glycophorin GalNAc-Ser/Thr residues with galactose.
4

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

63%
Zdebska E., Adamczyk-Poplawska M., Koscielak J.
Acta Biochimica Polonica
|
2000
|
tom 47
|
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.
5

Determination of single monosugars bound to a peptide

63%
Krotkiewski H., Krotkiewska B.
Acta Biochimica Polonica
|
1997
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tom 44
|
nr 2
A method is described which allows detection and quantitative determination of single monosugar units bound O-glycosidically to a peptide. A glycoprotein or a glycopeptide is chemically degraded under the modified conditions of Carlson degradation (beta-elimination performed in weakly alkaline conditions in the presence of sodium borohydride). An aliquot of the neutralized reaction mixture, supplemented with an internal standard, is peracetylated, extracted and directly analyzed by g.l.c.-m.s. All the O-linked oligosaccharides split off from the peptide are derivatized, but under gas-liquid chromatography at 150-230 degrees C only monosugar peracetylated alditols reach the detector. By comparing the retention times of appropriate peaks with standards and by checking their mass spectra the monosugar alditols are unequivocally identified. The detectable amount of a reduced monosugar in the analyzed sample is about 0.3 microgram. Several glycoproteins were analyzed using this method. Free N-acetylgalactosaminitol was detected in the degradation products of human glycophorin A and ovine submaxillary mucin, additionally free galactitol was detected in the degradation products of glycophorin. This result suggests that some single galactose units, O-glycosidically linked to the peptide are present in human glycophorin A.
6

Identification of blood group A and B antigens in human glycophorin

63%
Podbielska M., Krotkiewski H.
Archivum Immunologiae et Therapiae Experimentalis
|
2000
|
tom 48
|
nr 3
7

Purification of human anti-TF [Thomsen-Friedenreich] and anti-Tn antibodies by affinity chromatography on glycophorin A derivatives and characterization of the antibodies by microtiter plate ELISA

63%
Duk M., Lisowska E.
Archivum Immunologiae et Therapiae Experimentalis
|
1998
|
tom 46
|
nr 2
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