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  • Artikel: DFG Deutsche Nationallizenzen  (2)
  • Digitale Medien  (2)
  • 1990-1994  (2)
  • Atomic, Molecular and Optical Physics  (1)
  • Preservation, kidney, numan  (1)
Datenquelle
  • Artikel: DFG Deutsche Nationallizenzen  (2)
Materialart
  • Digitale Medien  (2)
Erscheinungszeitraum
Jahr
  • 1
    ISSN: 1432-2277
    Schlagwort(e): Preservation, kidney, numan ; Kidney, preservation, human ; UW solution, kidney ; Euro-Collins solution, kidney ; ATP, kidney, human
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Differences in purine metabolism produced by three preservation solutions were studied by determining the adenine nucleotide (ATP, ADP, AMP, and IMP) and nucleoside (adenosine, inosine, and hypoxanthine) levels in human kidney cortical biopsies. Forty kidney allografts were studied using University of Wisconsin (UW) solution (n=20), Euro-Collins (EC) solution (n=12), and modified EC solution with mannitol (M;n=8). No significant differences were found between the three solutions studied with regard to ATP, ADP, or AMP changes. The mean ATP level (nmol/mg prot±SEM) at the end of preservation in the UW group was 2.7±0.3 nmol/mg, in the EC group 3.8±0.7 nmol/mg, and in the M group 2.3±0.4 nmol/mg. ATP 30 min after reperfusion in the UW, EC, and M groups was 5.7±0.8 nmol/mg, 6.4±1.0 nmol/mg, and 4.6±0.5 nmol/mg, respectively. However, an important difference appeared in the catabolic products determined. Kidneys perfused with UW solution had a significantly higher level of adenosine (2.6±0.6 nmol/mg), inosine (11.8±2.2 nmol/mg), and hypoxanthine (18.1±2.1 nmol/mg) at hypoxanthine of cold storage than those perfused with EC (0.4±0.1 nmol/mg, 2.0±0.8 nmol/mg, and 7.1±1.4 nmol/mg) and M solutions (0.2±0.05 nmol/mg, 0.5±0.1 nmol/mg, and 5.2±0.6 nmol/mg; P〈0.05). These levels returned to initial values 30 min postreperfusion and there were no differences with the EC or M solution groups at that time. Thus, the adenosine present in UW solution does not appear to be useful in recovering the adenine nucleotide pool at reperfusion. Moreover, it produces a marked increase in degradation products. Our findings do not support the beneficial metabolic effect of UW solution in terms of adenine nucleotide metabolism in comparison with simpler and less expensive preservation solutions like EC.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    New York, NY : Wiley-Blackwell
    International Journal of Quantum Chemistry 39 (1991), S. 767-786 
    ISSN: 0020-7608
    Schlagwort(e): Computational Chemistry and Molecular Modeling ; Atomic, Molecular and Optical Physics
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: Electronic aspects of the catalytic mechanism of liver alcohol dehydrogenase (LADH) are studied with the help of ab initio analytical gradient SCF MO methods. Three points are considered: (i) role of the catalytic zinc; (ii) geometry and electronic structure of the transition state for the hydride transfer reactions; and (iii) factors affecting the energy gap for the hydride transfer step, namely, substrate binding to zinc, reaction field, and serine 48 effects on the potential energy profile. The coordination sphere of the catalytic zinc has been modeled with an ammonia molecule and two SH- groups; complexes with CH3O-, CH3OH, and CH2O have been studied; a (6, 2, 2, 2, 1/6, 2, 1/3, 2) basis set has been used for Zn++; a (5, 2, 1, 1/3, 2) was used for oxygen, carbon, and sulfur; and a (3, 1) was used for hydrogen atoms. The hydride step was studied with two model systems: pyridinium cation/1,4-dihydropyridine coupled to the CH3O-/CH2O reaction, and cyclopropenyl cation/cyclopropene coupled to the CH3O-/CH2O system. For the latter, the role of Ser48 has been studied at the supermolecule level. The calculation on the hydride transfer step has been done at a 4-31G basis set level. The results obtained shed new light on the sources of catalytic activity of liver alcohol dehydrogenases.
    Zusätzliches Material: 4 Ill.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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