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.
The recombination nearby large band-offset staggered lineup N-GaSb/n-GaInAsSb heterojunction was investigated by means of the electroluminescence and carrier lifetime measurements. It was demonstrated that the nature of recombination, tuning rate as well as relation between radiative and non-radiative recombination strongly depend on the N-n band-offset and that its increase improves the carrier localization on the N-n interface.
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