The hypothesis was tested that human donor livers with higher ATP content and energy charge achieve better results after hepatic transplantation. Biopsies were obtained from 25 donor livers immediately prior to implantation and analyzed for adenine nucleotides using high-performance liquid chromatography. The results were correlated with organ histology, transplant function and outcome. Significantly higher concentrations of ATP (4.22 +/- 2.87 vs. 0.71 +/- 0.69 nmoles per mg protein, p less than 0.01), ADP (8.75 +/- 2.96 vs. 4.49 +/- 1.95 nmoles per mg protein, p less than 0.01) and energy charge (0.43 +/- 0.15 vs. 0.21 +/- 0.04, p less than 0.02) were found in successful (n = 20) relative to failed (n = 5) livers. No significant differences were found in AMP, xanthine or hypoxanthine for the two groups, although the average values were higher in failed livers. Fifteen recipients with liver ATP concentration above 2 nmoles per mg protein and energy charge above 0.3 recovered well. Five other successful patients with lower ATP concentration (0.70 +/- 0.39 nmoles per mg protein) and energy charge (0.20 +/- 0.03) had postoperative courses complicated by infection or prolonged hyperbilirubinemia. In five patients whose livers failed, all had low ATP content and energy charge. Of these, three received a replacement liver and two died shortly after the transplantation. The study demonstrates a direct correlation between high ATP content and good posttransplant outcome.
Aerobic exercise training was found to be an effective means in inducing plasma levels elevation of the antioxidative, antiatherogenic paraoxonase in patients with coronary artery disease, and particularly in female patients.
Resonance Raman spectral changes in ferricytochrome c as a function of pH between 6.7 and 1.0 are reported and the structural implication is discussed in terms of the "core-expansion" model advanced by L. D. Spaulding et al. [(1975) J. Am. Chem. Soc. 97, 2517]. The data are interpreted as indicating the iron in high-spin ferricytochrome c (at pH 2.0) with two water molecules as axial ligands lies in the plane of the porphyrin ring. At pH 1.0 there is a different high-spin form of cytochrome c which has an estimated iron out-of-plane distance of approximately 0.46 A. The effect of a monovalent anion at pH 2.0 is to produce a thermal spin mixture with predominant low-spin species. Excitation at approximately 620 nm in acid cytochrome c (pH 2.0) enhances only three depolarized ring vibrations at 1623, 1555, and 764 cm-1. Marked enhancement of depolarized modes relative to polarized and anomalously polarized modes is attributed to the vibronic coupling between porphyrin pi leads to pi and porphyrin pi leads to iron (dpi) charge-transfer states.
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