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  • 1
    Electronic Resource
    Electronic Resource
    Altered frequency of initiation sites of DNA replication in Werner's syndrome cells (1982)
    Springer
    Human genetics 〈Berlin〉 60 (1982), S. 365-368 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary DNA replication of cultured fibroblasts of early passage derived from Werner's syndrome (adult progeria) patients and from normal subjects were compared by DNA fiber autoradiography. The frequency of replication initiation was decreased in Werner's syndrome cells derived from five patients compared with that in normal cells derived from three persons of different ages. The rate of DNA chain elongation did not differ between Werner's syndrome cells and normal cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00569220
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  • 2
    Electronic Resource
    Electronic Resource
    The mode of genetic transmission of a gouty family with increased phosphoribosylpyrophosphate synthetase activity (1981)
    Springer
    Human genetics 〈Berlin〉 58 (1981), S. 322-330 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The mode of genetic transmission of gout and increased activity of phosphoribosylpyrophosphate synthetase (PRPPS) was studied in one family. Among 15 members of Family F, two male members had gout and had PRPPS activity of erythrocyte lysates three times higher than normal subjects. Five female members had activity 2.5 times higher than normal. The difference between the activities of male and female affected members was statistically significant (P〈0.05). To examine the genetic trait of this abnormal PRPPS, the incorporation of 3H-adenine into erythrocytes or lymphocytes was studied using autoradiography. The number of grains which show the uptake of labeled adenine into cells revealed a normal distribution pattern in two normal persons and in two male patients, and a mixed pattern of the two cell populations in two female affected members. These results suggested mosaicism in female members and X-linked dominant transmission of this trait. Thermal inactivation of PRPPS of an affected female was intermediate between that from a normal subject and that from the affected males. This result showed the heterogeneity of the PRPPS from the hemolysate of an affected famale. The genotype of PRPPS on the X-chromosome was assumed and the lod score between PRPPS and Xg was also estimated. From these findings and electrophoretical study, it was suggested that the abnormal enzyme was a mutant enzyme transmitted in an X-linked dominant trait, and that the mutation occurred on the structural gene of the PRPPS.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00294932
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  • 3
    Electronic Resource
    Electronic Resource
    Structural changes in the oligosaccharide moiety of human IgG with aging (1998)
    Springer
    Glycoconjugate journal 15 (1998), S. 683-689 
    Details
    ISSN: 1573-4986
    Keywords: aging ; Asn-linked oligosaccharide ; glycosylation ; IgG ; galactose ; p-aminobenzoic acid ethyl ester ; ABEE, p-aminobenzoic acid ethyl ester ; IgG, IgA, and IgM, immunoglobulin G, A, and M,respectively ; HPLC, high performance liquid chromatography ; RA, rheumatoid arthritis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract In order to elucidate the relationship between glycosylation of IgG and aging, oligosaccharide structures of human IgG purified from sera of men and women aged 18 to 73 years were investigated. Oligosaccharides were liberated quantitatively from IgG by hydrazinolysis followed by N-acetylation and were tagged with p-aminobenzoic acid ethyl ester. The oligosaccharide structures were then analyzed by HPLC in conjunction with sequential exoglycosidase digestion. All IgG samples were shown to contain a series of biantennary complex type oligosaccharides which consisted of ±Galβ1-4GlcNAcβ1-2Manα1-6(±GlcNAcβ1-4)(±Galβ1-4GlcNAcβ1-2Manα1-3)Manβ1-4GlcNAcβ1-4(±Fucα1-6)GlcNAc and their mono- and di-sialo glycoforms in different ratios. In female IgG samples only, the incidence of non-galactosylated oligosaccharides with non-reducing terminal GlcNAc residues increased with aging (r〉0.8), whereas that of digalactosylated oligosaccharides decreased (r〈−0.8). A weaker correlation was observed between aging and the incidence of neutral and monosialo oligosaccharides in female IgG (r:0.461 and r=−0.538, respectively) and between aging and the incidence of oligosaccharides with a bisecting GlcNAc in both male and female IgG samples (r=0.566 and r=0.440, respectively). In addition, a significant change with aging in the galactosylation of IgG oligosaccharides was observed in females in their thirties, fifties, and sixties (p〈0.02, p〈0.01, and p〈0.04, respectively). These findings may contribute to our understanding of autoimmune diseases such as rheumatoid arthritis in which glycosylation is involved.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006936431276
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  • 4
    Electronic Resource
    Electronic Resource
    Detection of disease-specific augmentation of abnormal immunoglobulin G in sera of patients with rheumatoid arthritis (1998)
    Springer
    Glycoconjugate journal 15 (1998), S. 929-934 
    Details
    ISSN: 1573-4986
    Keywords: immunoglobulin G ; rheumatoid arthritis ; rheumatoid factor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Galactose-free immunoglobulin G (IgG), which is known to be higher in the sera of patients with rheumatoid arthritis, was prepared from IgG of healthy volunteers using enzymes. Its reactivity to lectins was analyzed. The galactose-free IgG showed no reactivity to Ricinus communis agglutinin 120 but displayed greater reactivity to concanavalin A and Lens culinaris lectin than did intact human IgG. Then, IgG in serum samples was bound to protein A immobilized on a nitrocellulose membrane, and its reactivity to biotinylated concanavalin A was measured with streptavidin-conjugated horseradish peroxidase. When the reactivity to concanavalin A of IgG in sera from healthy individuals and patients with rheumatoid arthritis (RA), osteoarthritis, systemic lupus erythematosus, or hepatic disease was compared, higher levels were shown in patients with RA, notably in 60% of the seronegative patients and 80% of the early phase patients. Therefore, it was suggested that augmentation of the abnormal IgG in sera was highly specific to patients with RA and that this novel serum test could be very useful for an accurate diagnosis of this disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006971318736
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    Paper (German National Licenses)
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