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  • Springer  (5)
  • 1975-1979  (5)
  • 1970-1974
  • 1920-1924
  • 1905-1909
  • 1979  (5)
  • 1
    Electronic Resource
    Electronic Resource
    Complementation of genetic disease: A velocity sedimentation procedure for the enrichment of heterokaryons (1979)
    Springer
    Somatic cell and molecular genetics 5 (1979), S. 1013-1029 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Methodology is described to enrich for heterokaryons after mammalian cell fusion. A heterogeneous cell mixture can be separated on a Sta-Put apparatus into fractions of uniform size cells by sedimentation through a 1% bovine serum albumin-5% Ficoll gradient. Unfused RAG and LM/TK− cells, differing by 10% in diameter, have been sorted by size; following fusion, larger and faster sedimenting cells were shown to be hybrids. This methodology can be utilized in genetic complementation studies of human genetic diseases where selection procedures for proliferating hybrids do not exist. When fibroblasts from individuals with Tay-Sachs disease [deficient in hexosaminidase A (HEX A−)] and Sandhoff-Jatzkewitz disease (HEX A− and HEX B−) are fused, HEX A is generated, demonstrating complementation of two different mutations. After Sta-Put fractionation, the HEX A complementation product was associated with the faster sedimenting multinuclear cells and not with the mononuclear parental cells. This methodology will facilitate detection of genetic differences in fibroblasts from related inherited disorders.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01542657
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Bioautographic visualization of aminoacylase-1: Assignment of the structural geneACY-1 to chromosome 3 in man (1979)
    Springer
    Somatic cell and molecular genetics 5 (1979), S. 11-21 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A bioautographic assay was developed for the visualization of aminoacylase-1 (N -acylamino acid aminohydrolase, ACY-1; EC 3.5.1.14) after zone electrophoresis. Bioautography and species differences in electrophoretic mobility of ACY-1 made it possible to investigate the chromosome assignment of the gene for human ACY-1 using human—mouse somatic cell hybrids. Human ACY-1 segregated concordantly with β-galactosidase-A (βGAL A;EC 3.2.1.23) but showed discordant segregation with 32 other markers representing 23 linkage groups. The β GALA gene has been previously assigned to chromosome 3. From this evidence and confirming chromosome analyses, ACY-1has been assigned to chromosome 3. A genetic polymorphism in the electrophoretic mobility of ACY was observed in mouse strains, demonstrating that this enzyme can be mapped in genetic crosses of Mus musculus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01538782
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  • 3
    Electronic Resource
    Electronic Resource
    Genetics of the cell surface: Assignment of genes coding for external membrane proteins to human chromosomes 10 and 14 (1979)
    Springer
    Somatic cell and molecular genetics 5 (1979), S. 281-301 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Using somatic cell hybridization gene mapping methodology, genes coding for human cell-surface proteins have been assigned to specific chromosomes. Lactoperoxidase-catalyzed iodination was employed to label external membrane proteins in cell hybrids between mouse and human cultured cells. Mouse and human external membrane proteins were separated by sodium dodecylsulfate-polyacrylamide gel electrophoresis. After electrophoresis, external membrane proteins were identified by autoradiography. An external membrane protein of 130,000 molecular weight (EMP-130) segregated concordantly with glutamic oxaloacetic transaminases (GOTs, EC 2.6.1.1), an enzyme marker encoded on chromosome 10. External membrane proteins of 195,000 and 175,000 molecular weight (EMP-195 and EMP-175) segregated concordantly with nucleoside phosphorylase (NP, EC 2.4.2.1), an enzyme marker encoded on chromosome 14. Limited proteolysis of the 195,000 and 175,000 molecular weight proteins suggests that these two proteins are modified forms of each other and are encoded by the same locus. These findings demonstrate the mapping of human genes coding for external proteins EMP-130 and EMP-195 to chromosomes 10 and 14, respectively. Chromosome analyses of cell hybrids supported these assignments.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01538843
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  • 4
    Electronic Resource
    Electronic Resource
    GM1-gangliosidosis: Chromosome 3 assignment of theβ-galactosidase-A gene (β GAL A ) (1979)
    Springer
    Somatic cell and molecular genetics 5 (1979), S. 147-158 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The structural gene (βGALA) coding for lysosomal β-galactosidase- A (EC 3.2.1.23) has been assigned to human chromosome 3 using man-mouse somatic cell hybrids. Human β-galactosidase-A was identified in cell hybrids with a species-specific antiserum to human liver β-galactosidase-A. The antiserum precipitates β-galactosidase-A from human tissues, cultured cells, and cell hybrids, and recognizes cross-reacting material from a patient with GM1 gangliosidosis. We have analyzed 90 primary man-mouse hybrids derived from 12 separate fusion experiments utilizing cells from 9 individuals. Enzyme segregation analysis excluded all chromosomes for βGALA assignment except chromosome 3. Concordant segregation of chromosomes and enzymes in 16 cell hybrids demonstrated assignment of βGALA to chromosome 3; all other chromosomes were excluded. The evidence suggests that GM1 gangliosidosis is a consequence of mutation at this βGALA locus on chromosome 3.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01539157
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  • 5
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    The use of body hydrogen as an internal standard in the measurement of nitrogen in vivo by prompt neutron capture gamma-ray analysis (1979)
    Springer
    Details
    Publication Date: 1979-03-01
    Print ISSN: 0236-5731
    Electronic ISSN: 1588-2780
    Topics: Chemistry and Pharmacology , Energy, Environment Protection, Nuclear Power Engineering
    Published by Springer
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