BACKGROUND: Cardiac output (CO) and systemic vascular resistance (SVR) are important hemodynamic parameters in emergency patients and for clinical early goal-directed therapy. This study evaluated the feasibility of CO and SVR determination using preclinical continuous wave Doppler ultrasound in a helicopter emergency medical service (HEMS) on emergency patients presenting with or without thoracic pain as a pilot observational study. METHODS: Forty-four consecutive medical emergency patients (62.8 +/- 22 years of age, 23 males) were classified at the scene as with (15 patients, 69 +/- 14 years of age, 40% male) or without (29 patients, 60 +/- 25 years of age, 59% male) thoracic pain by an emergency physician. Hemodynamic parameters were determined based on continuous wave Doppler noninvasively (USCOM, Sydney, Australia): stroke volume (SV), CO, cardiac index (CI), minute distance (MD), and SVR. RESULTS: Noninvasive SV, MD, CO, CI, and SVR determination is feasible using preclinical ultrasound in HEMS. Thoracic pain patients had higher SVR (2,709 +/- 891 vs 1,499 +/- 661 dyne*sec*cm-5) and lower CO/CI (3.37 +/- 1.1 vs 5.06 +/- 2.9 L/min, CI: 1.67 +/- 0.58 vs 3.18 +/- 1.34 L/min/m2) as well as a reduced aortic minute distance (11.2 +/- 3.3 m/min vs 19.1 +/- 8 m/min, P = .001) than patients without thoracic pain. Highest cardiac outputs were measured during and within 30 minutes after seizures (n = 5, 7.5 +/- 3.05 L/min). The range of CO measured in six cardiopulmonary resuscitation patients was 2.7 to 12 L/min; the level of CO was not associated with the establishing of sustained circulation. CONCLUSIONS: Determining SV, CO/CI, and SVR in different emergency situations in HEMS using rapid CW Doppler ultrasound is feasible. Thoracic pain patients have increased SVR and lower CO/CI and reduced aortic minute distance than do non-thoracic pain patients in the preclinical setting.

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PubMedDate not supplied

Energy-linked pyridine nucleotide transhydrogenase activity in photosynthetically grown Rhodopseudomonas palustris.

Rhodopseudomonas palustris (ATCC 17001) develops energy-dependent NADP+ transhydrogenase activity while growing photosynthetically on thiosulfate, formate, or acetate as the electron donors. The enzymatic activity is present in the supernatant fraction S-144 000. -- As reported, this fraction contains small membrane fragments but no closed vesicles and was shown to drive energy-dependent reversed electron flow as well as an aerobic respiratory electron transport. The energy-dependent transhydrogenase reaction in this fraction can be driven either by ATP, ADP, or inorganic pyrophosphate, but also by acetyl phosphate or acetyl-coenzyme A in the presence of orthophosphate. -- Arsenate acts as an inhibitor and decreases preferentially the acetyl-coenzyme A-dependent and the acetyl phosphate-driven reaction; whereas, oligomycin inhibits preferentially the ATP- and the acetyl phosphate-dependent reactions. -- Acetate kinase and a phosphotransacetylase are operative in S-144 000.

Acetates↗

PubMedDate not supplied

Respiratory electron flow and ATPase system in photosynthetically grown Rhodopseudomonas palustris.

Rhodopseudomonas palustris is grown photosynthetically on thiosulfate. As pointed out earlier, the chromatophore deficient cell-free fraction S-144,000 catalyzes the thiosulfate-linked ATP-dependent reversal of electron transfer in anaerobiosis, thus providing reducing equivalents in the form of NADH. Under aerobic conditions, this fraction also catalyzes the oxidation of NADH, ferro-cytochrome c, or ascorbate. ATP, ADP, and PPi are active in retarding the aerobic electron flow. The electron retardation is stimulated by the addition of Mg2+ due to a Mg2+-stimulated ATPase present. The ATPase system in S-144,000 hydrolyzes ATP, ADP, and PPi. Similarly, ATP or ADP, or even PPi can function as energy sources in order to achieve the reduction of pyridine nucleotide. The ATPase turnover is diminished by NADH or NAD+. Admixture of ascorbate results in an increased ATPase activity. Exactly the enhanced amount of adenine nucleotide hydrolysis caused by the addition of ascorbate is inhibited by cyanide.

Adenine Nucleotides↗