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  • 1
    Electronic Resource
    Electronic Resource
    Are abundant proteins less variable? (1980)
    [s.l.] : Nature Publishing Group
    Nature 284 (1980), S. 511-512 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THE analysis of enzymes using gel electrophoresis and specific activity stains has revealed extensive genetic diversity in man and other species. At least 25% of the genes which determine enzyme structure are variable and the average level of heterozygosity per gene locus detectable by conventional ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/284511a0
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  • 2
    Electronic Resource
    Electronic Resource
    Genetic variants in 2-D (1978)
    [s.l.] : Nature Publishing Group
    Nature 272 (1978), S. 309-310 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] ELECTROPHORESIS is a method without equal for the detection of individual variation arising from base pair substitutions. It has the potential for detecting about a third of all single base mutations-namely those which give rise to amino acid substitutions resulting in a change of net protein ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/272309a0
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  • 3
    Electronic Resource
    Electronic Resource
    An autosomal transcript in skeletal muscle with homology to dystrophin (1989)
    [s.l.] : Nature Publishing Group
    Nature 339 (1989), S. 55-58 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] To isolate the full coding sequence of the dystrophin gene, cDNA clones were used to walk sequentially in an oligo(dT)-primed, fetal-muscle cDNA library14"15. When the library was screened with two contiguous Hindll DMD cDNA fragments (D1.2 and D0.6, Fig. 1) that encode the final C-terminal domain ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/339055a0
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  • 4
    Electronic Resource
    Electronic Resource
    The expression of human glycerol-3-phosphate dehydrogenase in human/rodent somatic-cell hybrids (1985)
    Springer
    Biochemical genetics 23 (1985), S. 405-422 
    Details
    ISSN: 1573-4927
    Keywords: glycerol-3-phosphate dehydrogenase ; mitochondria ; mtDNA ; somatic-cell hybrids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Our previous studies using rodent/human somatic-cell hybrids suggested that the expression of human mitochondrial glycerol-3-phosphate dehydrogenase (GPDM) is dependent on the presence of human mitochondria. This has now been tested directly by analysis of GPDM activity in a series of nine hybrid-cell lines, four segregating human chromosomes and five losing rodent chromosomes (reverse segregants). The chromosome composition of the hybrids was deduced from analysis of biochemical markers and examination of G- and G11-banded metaphase spreads and the mitochondrial content was determined by Southern blot analysis, using cloned mouse and human mtDNA sequences as probes. We found that the mtDNA species present in these hybrids correlated exactly with the pattern of chromosome segregation such that the conventional hybrids contained rodent mtDNA and the reverse segregants human mtDNA. However, the pattern of GPDM expression was not directly correlated with the species of chromosomes or mitochondria present: all the hybrids showed strong rodem GPDM activity and two from each class of hybrid also showed human GPDM activity but the other hybrids were negative for human GPDM. We conclude that rodent GPDM readily integrates into human mitochondria, that the expression of rodent GPDM is not dependent on the presence of rodent mitochondria, and that GPDM is not coded by mtDNA. Human GPDM either is not capable of being inserted into the rodent mitochondrial membrane or is regulated in some way in the hybrid cells by an unidentified rodent factor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00499083
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  • 5
    Electronic Resource
    Electronic Resource
    Mouse carbonic anhydrase III: Nucleotide sequence and expression studies (1989)
    Springer
    Biochemical genetics 27 (1989), S. 17-30 
    Details
    ISSN: 1573-4927
    Keywords: λgt11 ; evolution ; hormonal regulation ; myoblasts ; isoelectric focusing ; DNA polymorphism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A cDNA for the mouse carbonic anhydrase, CAIII, has been isolated from a λgt11 expression library. The cloned cDNA contains all of the coding region (777 bp) and both 5′ untranslated (86-bp) and 3′ untranslated (217-bp) sequences. The coding sequence shows 87% homology at the nucleotide level and 91% homology, when amino acid residues are compared, with human CAIII. Protein and mRNA analyses show that CAIII is present at low levels in cultured myoblasts and is abundant in adult skeletal muscle and in liver. The marked sex-related differences in CAIII distribution, described for rat liver, are not seen in the mouse. Restriction fragment length polymorphisms usingTaqI andPstI are described which distinguish betweenMus spretus andMus musculus domesticus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00563015
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  • 6
    Electronic Resource
    Electronic Resource
    Characterization of human carbonic anhydrase III from skeletal muscle (1979)
    Springer
    Biochemical genetics 17 (1979), S. 837-854 
    Details
    ISSN: 1573-4927
    Keywords: carbonic anhydrase ; isozymes ; muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A third form of human carbonic anhydrase (CA III), found at high concentrations in skeletal muscle, has been purified and characterized. This isozyme shows relatively poor hydratase and esterase activities compared to the red cell isozymes, CA I and CA II, but is similar to these isozymes in subunit structure (monomer) and molecular size (28,000). CA III is liable to posttranslational modification by thiol group interaction. Monomeric secondary isozymes, sensitive to β-mercaptoethanol, are found in both crude and purified material and can be generated in vitro by the addition of thiol reagents. Active dimeric isozymes, generated apparently by the formation of intermolecular disulfide bridges, also occur but account for only a small proportion of the total protein and appear only when the concentration of CA III is particularly high.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00504307
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  • 7
    Electronic Resource
    Electronic Resource
    Distribution of CAIII in fetal and adult human tissue (1980)
    Springer
    Biochemical genetics 18 (1980), S. 843-849 
    Details
    ISSN: 1573-4927
    Keywords: carbonic anhydrase ; muscle ; fetal development
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Carbonic anhydrase III (CAIII), an enzyme recently shown by conventional electrophoresis to be muscle specific, has been quantitated by “rocket” immunoelectrophoresis. This more sensitive technique has shown that the enzyme is virtually specific to skeletal muscle, where it occurs at a level of 5mg/g, with trace levels in smooth muscle, cardiac muscle, and lung. In man there does not appear to by any correlation between CAIII levels and the proportion of red and white muscle fibers. The fetal development of CAIII has also been examined using immunoelectrophoresis, and the enzyme can be detected at 11 weeks' gestation. The CAIII level rises gradually up to 25 weeks, and there is then a more dramatic increase to reach approximately half adult level at birth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00500117
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  • 8
    Electronic Resource
    Electronic Resource
    Human succinate dehydrogenase: Biochemical and genetic characterization (1981)
    Springer
    Biochemical genetics 19 (1981), S. 741-756 
    Details
    ISSN: 1573-4927
    Keywords: isoenzymes ; membrane-associated proteins ; electrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A simple procedure for the preparation of soluble human succinate dehydrogenase is described. These preparations have proved suitable for analysis by zone electrophoresis, using a specific stain to detect activity after separation. In a survey of succinate dehydrogenase from various tissues and different individuals, no evidence for genetic heterogeneity due to the expression of either multiple loci or alternative alleles at the succinate dehydrogenase locus was found. However, epigenetic heterogeneity in both molecular size and charge was seen and various explanations for the occurrence of the isoenzymes are explored. Estimates of molecular size (93,300 ± 9100) suggest that the smallest active unit of succinate dehydrogenase accounts for the major part of the solubilized activity. Kinetic studies have shown that the apparent K m values for succinate (0.9mm) and PMS (0.4mm) are comparable to those previously described for the beef heart enzyme, and these parameters were not significantly altered when the enzyme was removed from the membrane milieu. However a marked non-succinate-dependent activation of the membrane-associated enzyme at 38C is apparently lost on solubilization, and this observation may have some bearing on earlier reports of an apparent decrease in V max on solubilization of succinate dehydrogenase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484006
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  • 9
    Electronic Resource
    Electronic Resource
    Regional localization of carbonic anhydrase genesCA1 andCA3 on human chromosome 8 (1987)
    Springer
    Somatic cell and molecular genetics 13 (1987), S. 173-178 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The human carbonic anhydrase isozymes represent a family of homologous proteins which are important in respiratory function, fluid secretion, and maintenance of cellullar acid-base homeostasis. Using somatic cell genetic techniques we have mapped two of the CA genes (CA1and CA3)to human chromosome 8. In situ hybridization data demonstrates that both CA1and CA3map to the same region (q13–q22) of chromosome 8.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01534697
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  • 10
    Electronic Resource
    Electronic Resource
    Trypanosoma (Schizotrypanum) species from insectivorous bats (Microchiroptera): characterization by polypeptide profiles (1982)
    Springer
    Systematic parasitology 4 (1982), S. 155-168 
    Details
    ISSN: 1573-5192
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary 1. The technique of sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) has been evaluated as a method for the characterization of trypanosomes. 2. Twenty-five populations, including seven clones, isolated from bats in Europe, Canada and Latin America could be grouped into eight subpopulations having similar polypeptide profiles. We propose to designate such subpopulations by the term ‘peptideme’. 3. Our peptidemes were compared with the previous classification, obtained by DNA buoyant density (Newton, 1976), isoenzym electrophoresis and morphological studies (Baker et al., 1976, 1978; Baker & Miles, 1979) as follows: 4. Peptideme 1 corresponded with Trypanosoma dionisii dionisii and peptideme 2 with T. d. breve and T. Hedricki. However, peptidemes 1 and 2 had some common shared characters. 5. Peptideme 3 corresponded with T. myoti and peptideme 4 with strain Z of T. cruzi marinkellei. Again, peptidemes 3 and 4 had some shared characters and these also shared some characters with peptidemes 1 and 2. 6. Peptideme 5 contained strains N2 and N6 of T. vespertilionis; the other strains of this species (482 and 482 clone 1), although sharing some common characters, were sufficiently different to enable us to group them as peptideme 6. 7. The remaining T. c. marinkellei strains were grouped into peptidemes 7 (B7, M1116, M1117, M1117X) and 8 (B34, M1909), although once again, these two peptidemes had some shared characters. Thus the peptideme method of classification of these trypanosomes corresponds well with the classification proposed previously but it is a more sensitive method and can recognize more subtle variation between the strains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00018999
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