ABSTRACT
The effects of extracorporeal shock wave lithotripsy (ESWL) were tested on four advanced generation implantable cardioverter-defibrillators (ICDs) in vitro and in vivo in two patients. During in vitro testing, advancement of nonsustained episode counters occurred in one device, and a set screw and power source cell loosened in another, which was connected to an external power source. No arrhythmias occurred during in vivo procedures, but programmed parameters were reset and elective replacement indicated after one procedure. ESWL can be performed safely in selected patients with ICDs, but testing should be performed afterwards to confirm satisfactory function and component continuity.
Subject(s)
Defibrillators, Implantable , Lithotripsy , Tachycardia, Ventricular/therapy , Ventricular Dysfunction, Left/therapy , Electrocardiography , Follow-Up Studies , Humans , Kidney Calculi/complications , Kidney Calculi/diagnostic imaging , Kidney Calculi/therapy , Male , Middle Aged , Radionuclide Imaging , Tachycardia, Ventricular/complications , Ventricular Dysfunction, Left/complicationsABSTRACT
The facultative phototrophic bacterium Rhodobacter capsulatus is capable of growth in a wide range of environmental conditions using a highly branched electron-transfer chain. During respiratory growth of this organism reducing equivalents are conveyed to oxygen via two terminal oxidases, previously called "cyt b410" (cytochrome c oxidase) and "cyt b260" (quinol oxidase). The cytochrome c oxidase was purified to homogeneity from a semiaerobically grown R. capsulatus strain. The purified enzyme consumes oxygen at a rate of 600 s-1, oxidizes reduced equine cyt c and R. capsulatus cyt c2, and has high sensitivity to cyanide. The complex is composed of three major polypeptides of apparent molecular masses 45, 32, and 28 kDa on SDS-PAGE. The 32- and 28-kDa proteins also stain with tetramethylbenzidine, indicating that they are c-type cytochromes. Partial amino acid sequences obtained from each of the subunits reveal significant homology to the fixN, fixO, and fixP gene products of Bradyrhizobium japonicum and Rhizobium meliloti. The reduced enzyme has an optical absorption spectrum with distinct features near 550 and 560 nm and an asymmetric Soret band centered at 418 nm, indicating the presence of both c- and b-type cytochromes. Two electrochemically distinct cyt c are apparent, with redox midpoint potentials (Em7) of 265 and 320 mV, while the low-spin cyt b has an Em7 value of 385 mV. The enzyme binds carbon monoxide, and the CO difference spectrum indicates that CO binds to a high-spin cyt b. Pyridine hemochrome and HPLC analyses suggest that the complex contains 1 mol of heme C to 1 mol of protoheme and that neither heme O nor heme A is present.(ABSTRACT TRUNCATED AT 250 WORDS)
