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  • Nucleosides  (1)
  • Venezuelan Indians  (1)
  • 1975-1979  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Conformation of the common purine (β) ribosides in solution: further evidence for a correlation between N-S state of the ribose moiety and syn-anti equilibrium (1975)
    Springer
    European biophysics journal 1 (1975), S. 121-137 
    Details
    ISSN: 1432-1017
    Keywords: Nucleosides ; Conformation ; HRNMR ; Relaxation ; NOE
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract The solution conformations of adenosine, guanosine and inosine in liquid ND3 have been determined by NMR. Comparison of the Karplus analysis of the proton HR spectra of the ribose moiety obtained in this solvent with the data from aqueous solutions of A and I proves that the conformations of the nucleosides are very similar in both liquids. From the analysis of the vicinal coupling constants of the ring protons it has been deduced that the S state C(2′)-endo is slightly preferred. The mole fraction in S approximates 0.6 for all three nucleosides. C-13 relaxation measurements have been applied in the determination of the correlation times for rotational diffusion. Only at temperatures below −40
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00539774
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  • 2
    Electronic Resource
    Electronic Resource
    Biochemical characterization of a red cell UMP kinase variant found in the Warao Indians of Venezuela (1978)
    Springer
    Biochemical genetics 16 (1978), S. 1085-1092 
    Details
    ISSN: 1573-4927
    Keywords: uridine monophosphate kinase ; erythrocyte enzymes ; genetic polymorphism ; Michaelis constant ; Venezuelan Indians
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract UMPK 3 is a rare variant of the polymorphic enzyme of human red cells, uridine monophosphate kinase. This homozygote phenotype was detected among the Warao Indians of Venezuela. The UMPK 1 and UMPK 3 enzymes were partially purified following the method described by Tend et al. (1976). The biochemical and kinetic parameters of both variants were studied in crude hemolysates and in partially purified enzymes. A comparison was made with the results previously reported by Teng for UMPK 1 and UMPK 2, and it was concluded that UMPK 3 seems to resemble the other two allelic gene products in Km values for UMP, CMP, and ATP but differs from them in electrophoretic mobility, pH optimum, and thermal stability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484529
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