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  • 1
    Electronic Resource
    Electronic Resource
    Genetic studies of human erythrocyte inosine triphosphatase (1969)
    Springer
    Biochemical genetics 3 (1969), S. 289-297 
    Details
    ISSN: 1573-4927
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The high concentrations of inosine triphosphate in human erythrocytes of some subjects has been related to a deficiency in intracellular inosine triphosphatase. Evidence has been presented for genetic transmission of this enzyme and for the existence of a homozygous-heterozygous relationship. Pedigree studies of individuals with erythrocyte ITPase deficiency suggest a Mendelian autosomal trait.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00521144
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    ITP pyrophosphohydrolase and idp phosphohydrolase in rat tissueA preliminary report of this work was presented at the 65th Meeting of the American Society of Biological Chemists, Minneapolis, 1974. (1975)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 86 (1975), S. 167-175 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The existence of a nucleoside triphosphate pyrophosphohydrolase specific for ITP has been demonstrated in the cytosol fraction of a variety of rat tissues. The enzyme, stable to moderate heat treatment, was present in erythrocytes as well as brain, heart, kidney, liver, lung, muscle, ovaries, spleen, testes and thymus. The specific activity of the enzyme ranges from 26 to 150 m̈moles/min/g protein. In addition, evidence is given for a heat labile nucleoside diphosphate (IDP) phosphohydrolase present in most rat tissues, and particularly high in the adrenal (137 m̈moles/min/g protein). An “ITP-IMP cycle” is proposed as a regulating mechanism for intracellular levels of ATP.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040860118
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Inosine di- and triphosphate synthesis in erythrocytes and cell extracts (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 99 (1979), S. 287-301 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The ability to synthesize inosinetriphosphate was demonstrated in blood cells as well as in a variety of tissue extracts in spite of the presence of ITP pyrophosphohydrolase. At the expense of having sub-optimal conditions, an assay system was selected that completely repressed the hydrolyzing enzyme, thus permitting the accumulation of ITP.In an attempt to define the biosynthetic pathway of ITP, and since guanylate kinase has been implicated in the formation of ITP, the rate of synthesis of ITP and GTP in cell extracts was compared.The comparison of the specific activities of the [14C]-labeled hypoxanthine and guanine moieties of the inosine and guanosine phosphates formed during incubation with [8-14C]-inosine and [8-14C]-guanosine respectively, revealed striking differences in the relative rates of isotope incorporation. Tentative mechanisms are proposed to explain these differences.The data obtained thus far does not discard the possibility that ITP may be formed by stepwise phosphorylation and (or) by direct pyrophosphorylation of IMP.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040990303
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  • 4
    Electronic Resource
    Electronic Resource
    Purification and properties of human erythrocyte inosine triphosphate pyrophosphohydrolase (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 98 (1979), S. 41-47 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Inosine triphosphate pyrophosphohydrolase from human erythrocytes was purified and characterized. The enzyme is highly specific for ITP and shows optimal activity in glycine buffer pH 9.6 and 50 mM MgCl2. The Km of the enzyme is 1.3 × 10-4, the Vmax = 1.2 × 10-9 and the Keq = 3.8 × 104. Human erythrocyte ITP pyrophosphohydrolase does not require SH compounds for activation. The enzyme is inhibited by Cd++, Co++, and Ca++ ions and by phydroxymercuribenzoate.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1040980106
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    Paper (German National Licenses)
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