A new rare phenotype of glycine-rich beta-glycoprotein.
A rare phenotype of serum glycine-rich beta-glycoprotein was found in a healthy Swiss woman. The rare gene product was also observed in three of her four sons.
Biomedical subjects
Publications and source records attributed to R Scherz.
A rare phenotype of serum glycine-rich beta-glycoprotein was found in a healthy Swiss woman. The rare gene product was also observed in three of her four sons.
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In a comparative study the presently known eleven allotypes of properdin factor B (Bf) were examined. Bf polymorphism consists of the two common alleles F and S, the two less common alleles F 1 and S 1 and seven further rare alleles. A variant designation has been proposed according to their relative electrophoretic mobility in comparison to the migration difference between the S and F 1 band. There rare variant alleles were redesignated: F 1.55, SO.45 and SO.7, which previously had been described as F 1.6, S 0.8 and S 1, respectively. Conversion studies did neither reveal variant mobility in the Bb nor in the Ba fragment of factor B in three of the rare alleles. This finding confirms the earlier report on one of the variants, possibly suggesting the existence of a so far unknown third clearing fragment.
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Human sera of different categories were screened for antibodies against IgA. A surprisingly high incidence of antibodies was observed. All of these antibodies were of restricted specificity, i.e. able to react with one or a few individual IgAs from a panel of eight myeloma proteins used in the screening. In one serum of a patient with selective IgA deficiency an antibody against the allotype A2m(1) was found. Some of the antibodies were shown to belong to the IgG class. The IgA, IgG and IgM content of the antibody-containing sera was generally increased. Two different antibodies which both reacted with the same individual IgA were studied in detail. The antigen involved could not be detected in normal Caucasian sera but was detectable in some sera of patients with IgA, IgG, IgM or IgD paraproteinemia. The antigenic site was located on the light chain of the Ig molecule but no correlation with either the light chain type or the genetically determined Inv factor was evident.
Gm phenotypes and IgG subclass levels were determined in the sera of 68 patients with neuroblastoma. The frequency of the uncommon phenotypes Gm(a+,f+,g-,b+) and Gm(a+,f+,g+,b-) was found to be significantly higher in the neuroblastoma group than in normal blood donors (p less than 0.001). IgG subclass concentrations in the nine sera with uncommon Gm phenotypes and in the sera of neuroblastoma patients were inconspicuous.
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The enzyme galactose-1-phosphate uridyl transferase (E.C.2.7.7.12), which has an important function in the metabolism of galactose, exists in multiple molecular forms. The different phenotypes are genetically determined. They can be distinguished according to their electrophoretic mobility. The enzymatic activity of the different gene products varies within certain limits. A new phenotype of the enzyme has been detected in the red cells of a healthy individual. The electrophoretic migration of this phenotype is slower compared to the wild type and its enzymatic activity is lower, but still sufficient as not to cause galactosemia. An extensive family study revealed that the rare gene is inherited according to mendelian law. Independently the same gene product has been detected in two other, nonrelated individuals out of a total of 1668 samples tested. The gene frequency can therefore be estimated to 0.0009 in the Swiss population. We suggest that the new type be called Berne variant of galactose-1-phosphate uridyl transferase.
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Immunofluorescence studies were performed on bone marrow samples from 21 individuals with normal or slightly elevated serum IgG levels. On the average, 40.7 percent of the IgG-positive plasma cells contained molecules of the subclass IgG; 30.6 percent had intracellular IgG2; 21.7 percent, IgG3, and 7.0 percent, IgG4. These figures were compared to the relative serum IgG subclass concentrations. The principal finding was the discrepancy between the high relative number of IgG-3 producing bone marrow plasma cells and the low relative IgG3-producing bone marrow plasma cells and the low relative IgG3 serum concentration (5.5 percent of the total IgG). It was explained by the short biologic half-life of molecules of this subclass.