Fucosidosis: clinical, pathologic, and biochemical studies of five patients.
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Biomedical subjects
Publications and source records attributed to P Sturgeon.
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Salivas with various phenotypes were analyzed for chemical components and blood group activity after ultracentrifugation. Active blood group substances were isolated from saliva in the pellet form by sedimentation. Both the supernatant and the pellet suspended in original volume were studied for content of fucose, total hexose, protein, and sialic acid and the presence of blood group activity. Paper chromatography of these saliva pellets after acid hydrolysis demonstrated fucose, galactose, glucosamine and galactosamine. A Lewis negative non-secretor showed decreased fucose on the paper while a non-secretor Lewis positive Le(a + b - x +) saliva showed less fucose on chemical analysis. Immunodiffusion studies with the lectin Dolichos biflorus showed precipitation lines with A substance from saliva and with purified A blood group substance. Goat anti-Lea and goat anti-Leb serum produced two precipitin lines against Lea substance and one line against Leb substance present in non-secretor and secretor salivas, respectively. In addition, there was a line of identify among Lea saliva, purified Lea substance from saliva and purified Lea substance from ovarian cyst fluid.
In serial MNSs tests on blood samples from 211 Chinese, 10 Mi(a+) were found, 9 of which were shown to belong to Miltenberger cell class III (Mi-III); it was assumed by analogy that this also applies to the tenth. The frequency of Mi-III in this Chinese series is thus 4.7%, almost 500 times higher than in Whites. Seventy persons in the series were tested for the Stones antigen: 2St(a+) were observed. Attention is drawn to the 'variant N' reactions of M Mi-III blood: positive with Vicia graminea extract, weakly positive with rabbit, negative with human anti-N. The reactions can be a source of error in MN tests on Chinese bloods.
The group of conditions exhibiting diminished MN antigenicity, increased saline agglutinability, decreased electrophoretic mobility and reduced membrane content of sialic acid includes enzyme-treated cells, the hereditary MNSs variants Mk and Mg, En(a-) and the acquired condition of persistent mixed-field polyagglutinability. Here we report our studies on the above serological, chemical and biophysical properties of Mg, Mk and EnaEn? CELLS AND ON TWO ADDITIONAL HEREDItary variants, Miltenberger III and V, (Mi-III and Mi-V). The latter clearly fits into this group of conditions. On the other hand, Mi-III shows its kinship to the broad group of abnormalities of membrane glycophorin but it deviates from normal in the opposite direction. That is we find evidence of decreased saline agglutinability, increased electrophoretic mobility and of increased sialic acid content. Moreover, in the rare MsMi-III Mk phenotype, the opposing effects evident in the heterozygotes tend to balance out their serologic and physicochemical expressions in the double heterozygote.
Electrophoretic mobility, membrane sialic acid content and agglutinability by "incomplete" antisera against Rh-o, hr' and k antigens were determined for red blood cells in the course of treatment with trypsin, ficin and neuraminidase. Neuraminidase gradually produces a slight to moderate agglutinability as it reduced surface charge density in proportion to the amount of sialic acid removed. Proteases acted in two distinct steps. The first stage is characterized by the cells rapidly becoming highly agglutinable and by the unmasking of new negative charge as the first half of the sialic acid is removed. In the second stage the cells show a slight gain in agglutinability as surface charge is removed in proportion to sialic acid removal as in the case of neuraminidase. Neuraminidase-treated cells are considerably less agglutinable than cells reduced to the same zeta-potential by protease treatment. The greater efficacy of proteases compared to neuraminidase in making cells agglutinable could be because they not only reduce surface charge density but also increase antigen-antibody bond strength, render antigens more mobile in the membrane to allow clustering in regions of cell to cell antibody bridging and remove glycopeptide chains which may be causing steric hindrance to antigen-antibody binding or to cell-cell contact.
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