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Biomedical subjects

H Cleve

Publications and source records attributed to H Cleve.

At least 91 records · Page 5Linked to original sources

Inheritance of PiM subtypes. A study of 151 families with a total of 242 children and of 142 mother-child pairs.

Pi phenotypes were classified by isoelectric focusing in sera of 151 families with a total of 242 children and in sera of 142 mother-child pairs. The six common subtypes of PiM are genetically determined by three alleles named PiM1, PiM2, and PiM3. No exceptions to the postulated mode of inheritance have been found. The possibility of further heterogeneity of the intermediate variant PiM3 is discussed.

Alleles↗

The lectin-binding sites of the erythrocyte membrane components of horse, swine and sheep. Characterization by their molecular weights.

The membrane components of equine, porcine and ovine erythrocytes were separated by sodium dodecylsulfate polyacrylamide gel electrophoresis and subsequently incubated with the radioiodinated lectins from lentils (LCH), castorbeans (RCA), Phaseolus beans (L-PHA), gorse seeds (UEH-F) and from vineyard snails (HPA). The following individual glycoproteins could be labeled: gp 26, 33, 100 and 320 in horse erythrocytes, gp 24, 46, 75, 130 and 210 in swine and gp 24, 57, 100 and 210 in sheep erythrocytes.

Animals↗

The lectin binding sites on the plasma membrane components of human lymphoblastoid cell lines.

The plasma membrane components of five human B-cell lines and three human T-cell lines were separated by dodecyl sulfate polyacrylamide gel electrophoresis, incubated with the radioactive labeled lectins from lentil, castor bean, wheat germ, Phaseolus bean, peanut, gorse and the Roman snail and the molecular weights of the binding sites determined. The lentil, castor bean and wheat germ lectin bound to multiple components from molecular weights (Mr) 20 000 to 200 000 within the plasma membranes, whereas peanut lectin bound preferentially to glycoproteins of Mr 150 000 and 83 000 in B-cells, and 150 000 and 130 000 in T-cells. The gorse lectin bound to a 220 000 component in B-cells which was not labeled in T-cells.

B-Lymphocytes↗

The lectin binding sites on the membranes of the nuclear envelope, mitochondria and the cell surface of human lymphoblastoid cells.

The membranes of the cell surface, the endoplasmic reticulum, outer and inner mitochondrial leaflet and nuclear envelope were isolated from three human lymphoblastoid cell lines. Membrane components were separated by dodecyl sulfate polyacrylamide gel electrophoresis and the gels incubated with the radioiodinated lectins from lentil, castor bean, scarlet runner bean, gorse seed and Roman snail. After gel slicing and counting, the molecular weights of the lectin binding sites were determined. About 20 glycoproteins were identified as constituents of the plasma membrane, a similar glycoprotein distribution was observed in the endoplasmic reticulum. The outer mitochondrial membrane contained some impurities from the plasma membrane, the inner mitochondrial membrane lacked specific lectin receptors. Two prominent glycoproteins with molecular weights of 70 000 and 60 000 were identified with the castor bean lectin in the nuclear envelope.

Cell Line↗

Genetic studies on the Gc subtypes.

Gc subtypes were determined by immunofixation isoelectric focusing. In a family study involving 93 families with a total of 176 children, a three-allele model with six genotypes was confirmed. The distribution of Gc subtypes was studied in three populations from Europe and in a sample of Druzes from Northern Israel. Three new variant Gc types were observed.

Alleles↗

Refined mapping of the gene for glutathione reductase on human chromosome 8.

Activity of the enzyme glutathione reductase (EC 1.6.4.2) in erythrocytes and fibroblasts of a patient with karyotype 46, XY, del(8) (pter-p212:) was found to be in the normal range. With results from other laboratories, this allowed a more precise mapping of the gene for this enzyme in the region 8p2100-8p212.

Child↗

Analysis of the Gc polymorphism in human populations by isoelectrofocusing on polyacrylamide gels. Demonstration of subtypes of the Gc allele and of additional Gc variants.

For the study of the group-specific component (Gc) system, serum samples were examined by polyacrylamide gel electrophoresis and by a newly developed immunofixation isoelectrofocusing procedure. Thereby, a greater extent of polymorphic variation was revealed than was known previously. The allele Gc1 could be subdivided into the alleles Gc1F and Gc1S. The distribution of Gc1 subtypes was very different in three populations (Pygmies, Amerindians, and Pyreneans) examined. New variants of the Gc1 and Gc2 genes were also described in the Amerindians and in the Pygmy population, respectively.

Alleles↗

GcT (Toulouse): a fast variant of the groupspecific system in an Pyrenean family.

In the course of a genetic investigation carried out in a Pyrenean population, a family with a new allele of the Gc system was found. Electrophoretic analysis revealed a faster migrating variant with a double band pattern. Presumably, this variant represents a mutant of the Gc1 allele. The variant is transmitted as an autosomal codominant trait. This additional allele at the Gc locus is named GcT (TcToulouse).

Alpha-Globulins↗

The vitamin D binding of the common and rare variants of the group-specific component (Gc). An autoradiographic study.

The vitamin D3 binding properties of the common and rare Gc variants were examined. Vitamin D3 labeled with 14C was added to serum. Gc phenotypes were demonstrated autoradiographically following separation by immunofixation electrophoresis on agarose. This qualitative analysis did not reveal differences in vitamin D3 binding by the group-specific components of the common types Gc 1-1, Gc 2-1, and Gc 2-2. The double-band variants Gc Darmstadt, Gc Y/Ab, Gc Toulouse, Gc Norway, and Gc Caucasian were examined; the phenotypes Gc Ab-Ab, Gc Ab-1, Gc Ab-1, Gc Ab-2, Gc T-1, Gc T-2, Gc Norw-2, and Gc 1-Cau showed normal D3 binding. The double bands of Gc Darmstadt in the phenotype D-2 appeared somewhat weak. The single-band mutants Gc Wien, Gc Chippewa, Gc Opava, and Gc Z were analyzed; the phenotypes Gc W-1, Gc W-2, Gc Chip-1, Gc Chip-2, Gc 1-Op, Gc Op-2, Gc 1-Z, and Gc 2-Z showed normal D3 binding. A mutant in the Gc system with clearly defective vitamin D3 binding properties remains to be delineated.

Alpha-Globulins↗

Classification of alpha1-antitrypsin (Pi) phenotypes by isoelectrofocusing. Distinction of six subtypes of the PiM phenotype.

Pi phenotypes have been determined by isoelectrofocusing in a sample of 538 healthy individuals from Southern Germany. Further subdivision of the common PiM phenotype is described. A procedure for the delineation of six common subtypes is presented. It is assumed that the six subtypes are determined by three alleles which are provisionally called PiMa, PiMb, and PiMc. Their frequencies in this sample were 0.75, 0.06, and 0.15, respectively.

Alleles↗

New chromosomal malformation syndromes. I. Partial monosomy 8p. An attempt to establish a new chromosome deletion syndrome.

A mentally retarded 8-year-old boy with a de novo partial monosomy for the short arm of the No. 8 chromosome is described. Based on G-banding analysis, the patient's karyotype was identified in lymphocytes and skin fibroblasts as 46,XY,del(8) (pter leads to p21:). No chromosomal abnormalities were found in the phenotypically normal mother, father and sister of the propositus. Four further cases described in the literature indicate that partial monosomy of the short arm of the No. 8 chromosome might be associated with a syndrome characterized by the following stigmata: mental retardation, slow growth, high forehead, broad chest, wide-set nipples, pulmonary stenosis with atrial and/or ventricular septal defect, hypoplasia of the genitalia, dermatoglyphic stigmata.

Child↗

[Beta2-microglobulin: structure and function of an immunoglobulin-homologue (author's transl)].

The low molecular weight protein beta2-microglobulin can be isolated from urine and other biological fluids. There is structural homology of beta2-microglobulin with the immunoglobulins, in particular to the CH3 domaine of the IgG molecule. Beta2-microglobulin can be detected on the cell membrane of most cell types and is associated with the histocompatibility antigens in a non-covalent binding. The immunological function of beta2-microglobulin is unclear. Antibody against beta2-microglobulin inhibits the mitogen- and antigen induced lymphocyte proliferation as well as responder and stimulator cell function in the mixed lymphocyte culture. The lack of structural polymorphism of beta2-microglobulin argues against a direct receptor function. It is more likely that beta2-microglobulin exerts a receptor-coordinating effect on the various receptor systems.

Amino Acid Sequence↗

Isolation and partial characterization of the major glycoproteins of horse and swine erythrocyte membranes.

The major glycoproteins of horse and swine erythrocyte membranes were isolated and examined chemically and immunologically. The major glycoprotein of horse erythrocyte membranes had a molecular weight of 33 000 and consisted of 46.2% protein and 53.8% carbohydrate, of which 9.4% was hexose, 10.1% hexosamine and 33.7% sialic acid. This glycoprotein was associated with activity for the infectious mononucleosis heterophile antigen. There were two different major glycoproteins in swine erythrocyte membranes. One major glycoprotein had a molecular weight of 46 200 and consisted of 34.2% protein and 65.8% carbohydrate, of which 18% was hexose, 19% hexosamine and 27.2% sialic acid. This glycoprotein had phytohemagglutinin (Phaseolus vulgaris) binding activity. The other glycoprotein had a molecular weight of 29 000 and consisted of 50.4% protein and 49.6% carbohydrate, of which 6.4% was hexose, 7.0% hexosamine and 36.3% sialic acid. This glycoprotein had weak or absent phytohemagglutinin binding activity.

Amino Acids↗

Isolation and partial characterization of two minor glycoproteins from human erythrocyte membranes.

Two minor glycoproteins GP-II and GP-III, were isolated from human erythrocyte membranes and characterized chemically and immunologically. The chemical composition of GP-II and GP-III was similar: GP-II consisted of 81% protein and 19% carbohydrate of which 4.9% was hexose, 5.4% hexosamine and 7.8% sialic acid. GP-III consisted of 76% protein and 24% carbohydrate of which 7.6% was hexose, 7.2% hexosamine and 8.1% sialic acid. The amino acid composition of GP-II and GP-III was also similar. GP-II and GP-III, however, differed in chemical composition from the MN glycoprotein. GP-II and GP-III were associated with the blood group activities Ss, I and A, but not with the MN antigens. GP-III had higher blood group activities per mug of protein than did GP-II. The specific activities for the Ss blood group antigens were increased 3-10-fold by purificantion of GP-III from the aqueous phase of chloroform methanol extracts.

Amino Acids↗

ADA-7--a new allele.

A new ADA phenotype which is particularly susceptible to phenotypic changes following storage was observed. Family studies indicate that this type may be due to a new allele, ADA-7. The phenotype observed was classified as ADA 7-1.

Adenosine Deaminase↗