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  • Articles  (7)
  • Springer  (7)
  • 2015-2019
  • 1980-1984  (7)
  • 1905-1909
  • 1981  (5)
  • 1980  (2)
  • Medicine  (7)
  • 1
    Electronic Resource
    Electronic Resource
    Calmodulin-like activity in a mineralising tissue: The rat molar tooth germ (1981)
    Springer
    Calcified tissue international 33 (1981), S. 545-548 
    Details
    ISSN: 1432-0827
    Keywords: calmodulin ; calcium ; mineralisation ; tooth germ
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Calmodulin, a calcium binding protein, has been implicated in the regulation of many calcium-dependent biological processes. Since calcium has an important role in hard tissue genesis, both at intra- and extracellular levels, we anticipate that calcium binding proteins may modulate this process. The present study investigated a mineralising tissue, the rat molar tooth germ, to determine the presence of calmodulin-like activity. A heat-treated cell-free extract of tooth germs provided enhancement of Ca2+-dependent Mg2+-ATPase and 3′:5′-nucleotide phosphodiesterase activity. No enhancement occurred in the absence of calcium or in the presence of trifluoperazine. SDS-polyacrylamide gel electrophoresis of this extract revealed a protein band of approximately 18,000 mol. wt. These findings indicate the presence of calmodulin-like activity in rat molar tooth germs and support the proposal that calcium and calcium binding proteins, in particular calmodulin, have a major regulatory role in the biology of mineralising tissues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02409487
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  • 2
    Electronic Resource
    Electronic Resource
    Assignment of the glyoxalase II gene (HAGH) to human chromosome 16 (1981)
    Springer
    Human genetics 〈Berlin〉 58 (1981), S. 358-361 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The human and rodent forms of glyoxalase II (hydroxyacylglutathione hydrolase, HAGH) can readily be separated by starch gel electrophoretic procedures. Fifty-one human-rodent somatic cell hybrid clones were examined for their human HAGH and for human enzyme markers whose genes are encoced on each autosome and the X chromosome. Sixteen clones were also examined for their human karyotypes. Human glyoxalase II segregated only with chromosome 16, demonstrating that the gene is located on this chromosome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00282815
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  • 3
    Electronic Resource
    Electronic Resource
    Assignment ofLIPA, associated with human acid lipase deficiency, to human chromosome 10 and comparative assignment to mouse chromosome 19 (1981)
    Springer
    Somatic cell and molecular genetics 7 (1981), S. 345-358 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The genetics of lysosomal acid lipase (LIP) has been investigated in human-Chinese hamster and mouse-Chinese hamster somatic cell hybrids. Cellulose acetate electrophoresis of human fibroblast extracts demonstrated that LIP activity consists of three isozymes. A deficiency of LIP activity has been observed in Wolman's disease (WD), cholesterol ester storage disease (CESD), and I-cell disease (ICD); this deficiency was associated with only one LIP isozyme, LIPA. We have demonstrated concordant segregation between human LIPA and human chromosome 10 and its enzyme marker glutamate oxaloacetate transaminase-1 (GOT1) in cell hybrid clones. Previous evidence suggested the different mutations associated with WD and CESD to be in the structural gene which we assign to human chromosome 10, while a different gene, involved in the processing of LIPA, is altered in ICD. These results indicate that several types of gene products are involved in the final expression of LIPA. In mouse-Chinese hamster hybrid clones, mouseLip-1 (homologous to humanLIPA) was assigned to chromosome 19. Previously, mouseGot-1 has been assigned to chromosome 19. Thus, theLIPA-GOT1 linkage group has remained intact during the 80×106 years of evolution that separates humans and mice.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01538859
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  • 4
    Electronic Resource
    Electronic Resource
    The proopiocortin (adrenocorticotropin/β-lipotropin) gene is located on chromosome 2 in humans (1981)
    Springer
    Somatic cell and molecular genetics 7 (1981), S. 359-369 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The proopiocortin gene is located on chromosome 2 in humans. A 13-kb DNA fragment containing proopiocortin gene sequences was identified in human cells while proopiocortin-related gene sequences of 9.8 and 6.2 kb were present in mouse cells. In human-mouse cell hybrids which contained reduced numbers of human chromosomes and a complete set of mouse chromosomes, the 9.8- and 6.2-kb fragments were always present while the 13-kb fragment segregated with human chromosome 2 and the chromosome 2 enzyme markers acid phosphatase-1 (ACP1), malate dehydrogenase-1 (MDH1), and isocitrate dehydrogenase-1 (IDH1). Analysis of a single cell hybrid with a broken chromosome 2 indicates that the proopiocortin andACP1 genes are closely linked and in the distal region of the short arm of chromosome 2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01538860
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  • 5
    Electronic Resource
    Electronic Resource
    Expression of H1 histone genes in mouse-human somatic cell hybrids (1980)
    Springer
    Somatic cell and molecular genetics 6 (1980), S. 653-665 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The synthesis of H1 histones was studied in nine mouse-human somatic cell hybrid clones containing reduced numbers of human chromosomes. The entire human genome could be accounted for karyologically and by the use of functional assays for specific enzyme markers encoded by human chromosomes. Chromatographic resolution and peptide mapping of species-specific H1 histones failed to reveal human H1 histones to a level of about 1% of total in the nine clones. In addition to the species-specific extinction of human H1 histones, effects were seen on the quantity of mouse H1 histone subtypes produced in four of the nine clones. The remaining five clones produced H1 histones qualitatively and quantitatively identical with those of the mouse parent, which was common to all nine clones. The results suggest at least two levels of control for H1 histone gene expression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01538644
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  • 6
    Electronic Resource
    Electronic Resource
    Branched-chain aminotransferase deficiency in Chinese hamster cells complemented by two independent genes on human chromosomes 12 and 19 (1980)
    Springer
    Somatic cell and molecular genetics 6 (1980), S. 641-652 
    Details
    ISSN: 1572-9931
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Branched-chain aminotransferase (BCT) catalyzes the reversible transamination of the branched-chain α-keto acids to the branched-chainl-amino acids. Since branched-chainl-amino acids (l-isoleucine,l-leucine, andl-valine) are essential for cell growth, cells which lack BCT were unable to proliferate in media containing α-keto acids in place of the correspondingl-amino acids. CHW-1102, a Chinese hamster cell line, lacks BCT and does not grow in α-keto acid media. Somatic cell hybrids were made by the fusion of CHW-1102 (HPRT−) with several human cell lines and isolated on HAT medium. Growth assays of hybrid clones on α-keto acid selection media independent of the HAT selection medium indicated two cell hybrid phenotypes: either (1) the hybrid clone, like the parental CHW-1102, could not utilize α-keto acid media, or (2) the hybrid could proliferate on all three α-keto acid media. The ability of hybrid cells to proliferate on α-keto acid media correlated with the presence of either of two human genes which independently complemented the Chinese hamster deficiency. Two human genes, BCT1 assigned to chromosome 12 and BCT2 assigned to chromosome 19, were demonstrated to code for the expression of two molecular forms of BCT.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01538643
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  • 7
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    Assignment of the glyoxalase II gene (HAGH) to human chromosome 16 (1981)
    Springer
    Details
    Publication Date: 1981-10-01
    Print ISSN: 0340-6717
    Electronic ISSN: 1432-1203
    Topics: Biology , Medicine
    Published by Springer
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