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  • 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
    Efficient hybridization between Lycopersicon esculentum and L. peruvianum via embryo callus (1981)
    Springer
    Theoretical and applied genetics 59 (1981), S. 215-219 
    Details
    ISSN: 1432-2242
    Keywords: Interspecific hybridization ; Embryo callus ; Plant regeneration ; Lycopersicon esculentum ; Lycopersicon peruvianum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Embryo callus was produced in up to 12% of the undeveloped seeds of the interspecific cross L. esculentum cv. VFNT cherry x L. peruvianum LA1283-4, a cross which does not produce viable seeds. Plants were produced from 90% of those callus clones by regeneration and rooting. Evidence that these plants were hybrid includes morphology, isoenzyme patterns and fertility relations. Both diploid and tetraploid plants were produced, 40% of the regenerated callus clones producing at least one diploid plant. Thus, up to 4% of the undeveloped seeds plated for callus production eventually yielded diploid hybrid plants. In contrast, among 401 undeveloped seeds dissected, no embryos suitable for embryo culture were found. A backcross of the embryo callus hybrids to the L. esculentum parent has succeeded — producing, as expected, only undeveloped seeds; these undeveloped seeds have produced callus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00265495
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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
    The effect of additives on the morphology of zinc electrodeposited from a zinc chloride electrolyte at high current densities (1981)
    Springer
    Journal of applied electrochemistry 11 (1981), S. 677-683 
    Details
    ISSN: 1572-8838
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Electrical Engineering, Measurement and Control Technology
    Notes: Abstract There are advantages if zinc can be deposited electrochemically at high current densities. In order to improve the deposit at current densities exceeding 2000 Am−2, various additions were made to the electrolyte. It was found that proteinous additives produced planar deposits with a (10.2) (10.3) orientation and a current efficiency of around 85% in a small laboratory cell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00615170
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  • 6
    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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  • 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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