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  • Articles  (23)
  • Springer  (14)
  • Institute of Physics  (7)
  • Wiley-Blackwell  (2)
  • 1975-1979  (17)
  • 1965-1969  (6)
  • 1905-1909
  • Biology  (23)
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  • Articles  (23)
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  • 1
    Electronic Resource
    Electronic Resource
    The amino acid substitution and some chemical properties of a variant human erythrocyte carbonic anhydrase: Carbonic anhydrase IdMichigan (1967)
    Springer
    Biochemical genetics 1 (1967), S. 171-195 
    Details
    ISSN: 1573-4927
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Carbonic anhydrase IdMichigan, an electrophoretic variant of human red cell carbonic anhydrase I, was purified from erythrocytes obtained from an individual heterozygous for the trait. Primary structural analysis indicates that a lysine residue has exchanged for a threonine residue in the variant enzyme. After isolation, there was approximately 1.8 times as much normal as variant enzyme. Thermostability studies demonstrated that carbonic anhydrase Id was more thermolabile than the normal enzyme. The normal and variant enzymes showed no differences in specific carboxylesterase activity or CO2 hydratase activity. Utilizing the carboxylesterase activity toward β-naphthyl acetate, the normal and variant enzymes had similar Michaelis constants, pH profiles, and rates of inhibition by acetazolamide. Immunochemical studies did not demonstrate an antigenic difference for the variant enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00486517
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  • 2
    Electronic Resource
    Electronic Resource
    Phosphoglucomutase electrophoretic variants in the mouse (1969)
    Springer
    Biochemical genetics 3 (1969), S. 25-35 
    Details
    ISSN: 1573-4927
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The phosphoglucomutase (PGM) electrophoretic phenotype of the mouse (Mus musculus) consists of several distinct components which can be grouped into two major zones designated PGM-1 and PGM-2. Evidence presented here indicates that each zone is controlled by a single genetic locus denoted Pgm-1 and Pgm-2, respectively. Two variant forms segregated at the Pgm-1 locus. They were codominantly expressed and inherited as alleles at an autosomal locus. The alleles were termed Pgm-1 a (fast) and Pgm-1 b (slow). These alleles were separately fixed in a number of inbred strains of mice. Preliminary evidence based on wild mouse phenotypes indicates that variant forms also exist for PGM-2 which are inherited as alleles at an autosomal locus. Genetic linkage relationships have not been determined for these loci. PGM-1 variants and PGM-2 were expressed in mouse fibroblasts in vitro.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485972
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  • 3
    Electronic Resource
    Electronic Resource
    Intranuclear and cytoplasmic annulate lamellae in grasshopper spermatocytes (Genus Melanoplus) (1975)
    Springer
    Cell & tissue research 156 (1975), S. 475-482 
    Details
    ISSN: 1432-0878
    Keywords: Annulate lamellae ; Spermatocytes ; Grasshoppers ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Intranuclear and cytoplasmic annulate lamellae were studied in grasshopper spermatocytes (Melanoplus) with the electron microscope. Although cytoplasmic annulate lamellae were observed in all three species examined, intranuclear annulate lamellae were found in only one species. The intranuclear annulate lamellae encompass certain nuclear material adjacent to the nuclear envelope forming a vesicle that is extruded into the spermatocyte cytoplasm. In this same species, cytoplasmic annulate lamellae are seen contiguous with granular masses of varying size. These structures were noted as being morphologically indistinguishable from the “yolk nuclei” of dragonfly oocytes (Kessel and Beams, 1969; Kessel, 1973).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00225107
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  • 4
    Electronic Resource
    Electronic Resource
    Evolutionary evidence for a regulator gene controlling the lactate dehydrogenase B gene in rodent erythrocytes (1969)
    Springer
    Biochemical genetics 3 (1969), S. 525-536 
    Details
    ISSN: 1573-4927
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Erythrocyte and tissue lactate dehydrogenase (LDH) electrophoretic patterns of 26 rodent species from ten families were examined. The LDH B gene was observed to range in erythrocyte expression from species without detectable B subunits to those which predominantly expressed B subunits. However, the shift in erythrocyte B gene expression was not observed in the tissue LDH electrophoretic patterns between rodent species. Species which did not express erythrocyte B subunits, or only small quantities of B subunits, were restricted to the suborder Myomorpha. In erythrocytes of other rodent species, and most mammals, LDH B subunits are expressed equally or in excess of A subunits. The results suggest either structural differences in the LDH B gene between Myomorph and non-Myomorph rodents or a regulator gene which controls the expression of the B gene in Myomorph erythrocytes. Existing evidence favors the latter hypothesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00485474
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  • 5
    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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  • 6
    Electronic Resource
    Electronic Resource
    Polyethylene glycol-induced mammalian cell hybridization: Effect of polyethylene glycol molecular weight and concentration (1976)
    Springer
    Somatic cell and molecular genetics 2 (1976), S. 271-280 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The effects of polyethylene glycol (PEG) molecular weight and concentration on mammalian cell hybridization were studied. The peak hybridization-inducing activity with all grades of PEG from 400–6000 was found to occur in the concentration range of 50–55%. However, changes in concentration were seen to have different quantitative effects with different grades of PEG. For monolayer fusions, PEG 1000 at 50% seems to be the optimal combination of PEG molecular weight and concentration, in terms of both efficiency of hybridization and relative insensitivity to dilution effects.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01538965
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  • 7
    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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  • 8
    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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  • 9
    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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  • 10
    Electronic Resource
    Electronic Resource
    Galactose and glucose metabolism in galactokinase deficient, galactose-1-P-uridyl transferase deficient and normal human fibroblasts (1975)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 85 (1975), S. 569-577 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Despite the genetic interruption of the Leloir pathway both galactosemic patients and galactosemic fibroblasts can convert galactose to CO2 and TCA precipitable products, although at less than the normal rate. These observations stimulated investigations into the identity of the alternative metabolic routes which allow for galactose metabolism in the absence of in vitro galactose-1-P-uridyl transferase. Four lines of galactosemic cells, each without detectable gal-transferase, produced 14CO2 from [1-14C]-galactose (0.094 μmoles in 20 cc of medium) at approximately 39% ± 16% the rate of transferase positive cells over a 48-hour period. However, galactokinase deficient fibroblasts produced 14CO2 and TCA precipitable products from [1-14C] -galactose or [U-14C] -galactose at only 3% to 9% the rate of normal fibroblasts. Therefore it seems likely that galtransferase deficient fibroblasts must first synthesize galactose-1-P for further metabolism of galactose.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040850308
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