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Biomedical subjects

R Scherz

Publications and source records attributed to R Scherz.

At least 37 records · Page 2Linked to original sources

Characterization of various immunoglobulin preparations for intravenous application. I. Protein composition and antibody content.

In this comparative study we investigated 14 immunoglobulin (Ig) preparations for intravenous application; they were prepared by various manufacturers who used either placental or venous blood as the starting material. The pepsin- and plasmin-treated products and a preparation which, according to the manufacturer, was not degraded enzymatically, contained 17-86% of IgG split products. On the other hand, three chemically modified preparations, one preparation treated at pH 4, for products treated with poly(ethylene glycol) (PEG) and one preparation protected by albumin contained 90% or more of non-fragmented IgG. The IgG subclass distribution corresponded to the distribution of subclasses in normal serum only in the nonmodified and not enzymatically degraded preparations. All samples except one contained 0.1 mg/ml IgA or more, all contained only traces of IgM. No product had clinically relevant titers of irregular antibodies against erythrocyte antigens. The content of those antiviral and antibacterial antibodies that were tested for was similar in all preparations. Only the anti-HBs activity exhibited large variations. Some PEG-treated preparations showed an elevated prekallikrein activator (PKA) level, whereas all other preparations contained, if any, only traces of PKA.

ABO Blood-Group System↗

Isoelectric focusing of human red cell phosphoglucomutase (PGM1): phenotype distribution in the Swiss population - rare phenotypes.

Gene frequencies of PGM1 phenotypes as obtained by isoelectric focusing on polyacrylamide gel in the pH range from 4 to 8 were determined in 501 samples of Swiss blood donors. Results were in good agreement with the expected distribution according to the Hardy-Weinberg law. Frequencies were PGM1a1 = 0.6278, PGM1a2 = 0.1936, PGM1a3 = 0.1297, PGM1a4 = 0.0489. Comparison with other data of the white population showed no significant differences. Isoelectric points of regular and rare gene products were determined. Application of the method in routine paternity testing is discussed.

Adolescent↗

The nomenclature of properdin factor B allotypes.

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.

Alleles↗

Naturally occurring human antibodies with specificity for light chains of immunoglobulins.

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.

Antibodies, Anti-Idiotypic↗

Uncommon Gm phenotypes in sera from neuroblastoma patients.

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.

Adolescent↗

A new genetic variant of galactose-1-phosphate uridyl transferase.

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.

Adult↗

Cytoplasmic immunofluorescence of bone marrow plasma cells producing immunoglobulins of the four IgG subclasses.

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.

Adult↗