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1

Carbohydrate moiety of immunoglobulins in health and pathology

100%
Krotkiewski H.
Acta Biochimica Polonica
|
1999
|
tom 46
|
nr 2
Most of glycoproteins described so far, including immunoglobulins, are glycosylated during post-translational modifications of protein molecules. Current knowledge of the structure of sugar chains in immunoglobulin molecules and their biological role in health and pathology is reviewed.
2

In memoriam

63%
Zimecki M., Krotkiewski H.
Archivum Immunologiae et Therapiae Experimentalis
|
1999
|
tom 47
|
nr 1
3

Determination of single monosugars bound to a peptide

63%
Krotkiewski H., Krotkiewska B.
Acta Biochimica Polonica
|
1997
|
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.
4

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
5

Heterogenity of protein glycosylation analyzed by surface plasmon resonance

51%
Krotkiewska B., Buchaniewicz M., Jakubiak A., Krotkiewski H.
Acta Biochimica Polonica
|
2006
|
tom 53
|
nr Supplement 1
6

Building the prestige of Archivum Immunologiae et Therapiae Experimentalis: from a little known to an internationally recognized journal

51%
Krotkiewski H., Gorski A., Zimecki M.
Archivum Immunologiae et Therapiae Experimentalis
|
2018
|
tom 66
|
nr 6
7

The carbohydrate moiety of human glycophorin in CDG syndrome

51%
Krotkiewska B., Zwierz K., Krotkiewski H.
Acta Biochimica Polonica
|
1999
|
tom 46
|
nr 2
Human glycophorin, the major sialoglycoprotein of erythrocyte membranes, was isolated from erythrocytes of healthy individuals and four patients with CDG syndrome. Sugar analysis revealed lower carbohydrate content in three out of four CDG-glycophorin samples. In order to characterize closer the glycosylation differences between glycophorin samples in health and disease, reaction with four biotinylated lectins was performed, using ELISA procedure on polystyrene microplates. Results obtained so far strongly suggest that both N- and O-glycans of glycophorin are affected in CDG syndrome.
8

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

51%
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.
9

Mouse monoclonal IgA antibodies lack interchain disulfide bonds

51%
Krotkiewski H., Laskowska A., Krotkiewska B.
Archivum Immunologiae et Therapiae Experimentalis
|
1995
|
tom 43
|
nr 3-4
10

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

51%
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.
11

Professor Elwira Lisowska celebrates her 90th birthday

45%
Krotkiewski H., Czerwinski M., Jaskiewicz E., Wasniowska K., Kaczmarek R.
Archivum Immunologiae et Therapiae Experimentalis
|
2020
|
tom 68
|
nr 4
12

Studies on immunogenicity and antigenicity of baculovirus- expressed binding region of Plasmodium falciparum EBA-140 merozoite ligand

33%
Zerka A., Rydzak J., Lass A., Szostakowska B., Nahorski W., Wroczynska A., Myjak P., Krotkiewski H., Jaskiewicz E.
Archivum Immunologiae et Therapiae Experimentalis
|
2016
|
tom 64
|
nr 2
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