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  • 1
    Electronic Resource
    Electronic Resource
    The Histidine Decarboxylase (HDC) Gene of Tetrahymena Pyriformis is Similar to the Mammalian One. A Study of HDC Expression (1999)
    Springer
    Bioscience reports 19 (1999), S. 73-79 
    Details
    ISSN: 1573-4935
    Keywords: Histidine decarboxylase ; Tetrahymena ; gene sequencing ; evolution ; histamine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract RNA was isolated from Tetrahymena pyriformis GL and using human histidine decarboxylase (HDC) gene primers, the RT-PCR product was sequenced. A fraction containing 207 base pairs was compared to the published sequences of prokaryotic and mammalian (rat, mouse and human) HDC cDNA (exons). The HDC-cDNA fraction of Tetrahymena was similar to the mammalian cDNA-s and it was completely different from the prokaryotic HDC-gene. The results indicate the presence of a mammalian-like HDC-gene already in a unicellular eukaryote organism and demonstrates also that the divergence of the prokaryotic–eukaryotic common gene took place already at this low evolutionary level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1020102308791
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Immunocytochemical verification of the insulin receptor's specificity in the nuclear envelope of Tetrahymena. Comparison with receptors of the plasma membrane (1994)
    Springer
    Bioscience reports 14 (1994), S. 25-31 
    Details
    ISSN: 1573-4935
    Keywords: insulin receptor ; hormonal imprinting ; Tetrahymena ; nuclear envelope ; specificity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The unicellular Tetrahymena possess hormone receptors in the nuclear envelope similarly to higher rank animals. These receptors bind insulin and their specificity is detectable by monoclonal antibodies developed to insulin. The hormonal (insulin) pretreatment (imprinting) of the cell did not alter the binding capacity of the nuclear membrane, demonstrated by antibody-technique. The specific binding characteristics of the plasma membrane was demonstrated and this was significantly increased following imprinting. In the nucleus of Tetrahymena presence of insulin was not detected by immunocytochemical method.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01901635
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    A calcium-dependent protein kinase is present in tetrahymena (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 12 (1994), S. 221-226 
    Details
    ISSN: 0263-6484
    Keywords: Tetrahymena ; protein kinase ; phylogeny ; Ca-dependence ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A Ca2+-dependent protein kinase of Tetrahymena thermophila has been partially purified and characterized. The molecular mass of the enzyme is less than that of similar enzymes (for example protein kinase C), being about 55 kDa. After purification and in the presence of Ca2+ the enzyme activity increased. The promoter of protein kinase C (PKC) activity, phorbol myristate acetate (PMA), increased the activity while the protein kinase inhibitor H-7 decreased the activity of the enzyme. The experiments demonstrate the presence, activity and similarity to vertebrate enzymes of a protein kinase at a low level of phylogeny.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290120311
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Effect of vanadate and ouabain on insulin binding and insulin imprinting in Tetrahymena (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 10 (1992), S. 31-34 
    Details
    ISSN: 0263-6484
    Keywords: Insulin binding ; Tetrahymena ; vanadate ; ouabain ; imprinting ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Na-metavanadate and ouabain that act on Na+K+-ATPase had no influence on insulin binding to Tetrahymena immediately after treatment, but after 24 h considerably enhanced the binding capacity of generations of progeny. The increase in binding was of a similar magnitude to that elicited by insulin imprinting. Vanadate failed to increase the imprinting potential of insulin while ouabain even prevented insulin imprinting when administered together with insulin, but, did not affect imprinting when administered after insulin. By analogy with higher organisms it appears that inhibition of Na+K+-ATPase plays no role in the insulin-like effect of vanadate on the unicellular Tetrahymena, as judged also from the capacity to bind insulin of the generations of offspring.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290100106
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    Paper (German National Licenses)
    Fulltext
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