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1

Identification of blood group A and B antigens in human glycophorin

100%
Podbielska M., Krotkiewski H.
Archivum Immunologiae et Therapiae Experimentalis
|
2000
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vol. 48
|
issue 3
211-221
EN
Glycophorin A (GPA), the major sialoglycoprotein of human erythrocyte membranes, was isolated separately from blood group A and B erythrocytes using phenol-water extraction. After purification, performed as gel filtration in the presence of SDS, two glycophorin samples GPA-A and GPA-B were run, in duplicate, in SDS-PAGE and electroblotted onto Immobilon P. After staining with 1) anti-glycophorin antibody and 2) with relevant anti-blood group (A or B) antibody it was shown that the band pattern of the samples in each duplicate was the same. GPA-A and GPA-B samples were also degraded using Carlson degradation (-elimination in mild alkaline/strong reducing conditions) and from reaction products the fractions of O-glycans and N-glycans were isolated; they were used in hemagglutination inhibition test. It was shown that both sugar fractions derived from GPA-A did inhibit agglutination of blood group A erythrocytes by anti-A antibody, whereas oligosaccharide fractions derived from GPA-B inhibited agglutination of blood group B erythrocytes by anti-B antibody. These results, obtained using immunochemical methods, confirm the presence of blood group A and B determinants in the carbohydrate moiety of human glycophorin, derived from the blood group A or B erythrocytes, respectively.
2

Expression of human blood group antigens A and B in kidney and lung of some vertebrates

86%
Tomova E. S., Popov A. A., Sarafian V. S.
Folia Biologica
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2001
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vol. 49
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issue 3-4
251-257
EN
Human blood group antigens (BGA) are genetically determined glycoproteins found in many cells and tissues of different mammals. Their major biological functions are still undefined. There are few investigations analysing the evolutionary aspect of BGA tissue ditribution. The present study is aimed at examining the expression of human A and B antigens in the kidney and lung of some free-living vertebrates. The biotin-streptavidin-peroxidase immunostaining system was applied on kidney and lung paraffin sections derived from free-living representatives of five different vertebrate classes. Excluding the possibility of any non-specific staining by the application of inhibition tests, A and B antigens were demonstrated most constantly in epithelial cells of renal and respiratory tubules. They were also detected in chondrocytes of fish gills, in some muscular and endothelial cells. Single erythrocytes showed a positive cytoplasmic staining only in some higher vertebrates. Human BGA seem to be conserved carbohydrate structures with biological functions probably related to cell integrity and differentiation.
3

Genetic structure and phylogenetic relationships of the Polish Heavy Hors

86%
Iwanczyk E., Juras R., Cholewinski G., Cothran E. G.
Journal of Applied Genetics
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2006
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vol. 47
|
issue 4
353-359
EN
In this study a wide range of genetic markers (12 microsatellites, 7 blood-group loci, 10 blood-protein loci) and mitochondrial DNA (mtDNA) were used to assess genetic diversity in Polish Heavy horses. Three random samples were sequenced for 421 bp of the mitochondrial D-loop region, but no clear phylogenetic patterns were seen in mtDNA variation. Both heterozygosity and diversity levels are fairly high in Polish Heavy horses. In phylogenetic analysis the draught horses form a distinct cluster that pairs with the true pony breeds. Within this 'cold-blooded' group, the Polish Heavy Horse clusters most closely with the Posavina breed from Croatia and the Breton breed from France. From the standpoint of genetic conservation, the Polish Heavy Horse does not appear to be in jeopardy.
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