Thoracic epidural versus patient-controlled analgesia in elective bowel resections.

BACKGROUND: This study was undertaken to determine if thoracic epidural analgesia is of practical benefit after bowel resection. METHODS: Patients were prospectively randomized to receive either a thoracic epidural or patient-controlled analgesia for pain control after bowel resection. A standardized postoperative protocol was instituted after surgery. RESULTS: Pain scores were significantly lower in the epidural group. Return of bowel function, and interval to discharge was not different between groups. Cost and complication rates were significantly higher in the epidural group. CONCLUSIONS: Although pain scores were significantly lower in the epidural group, this did not translate into a quicker return of bowel function or earlier discharge of the patient. Furthermore, the epidural group had a significantly higher complication rate and cost. Therefore, while thoracic epidural analgesia provides superior pain control, it does not offer a significant advantage over patient-controlled analgesia in return of bowel function after bowel resection.

Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state.

We demonstrate that high-resolution multidimensional solid state NMR methods can be used to correlate many backbone and side chain chemical shifts for hydrated micro-crystalline U-13C,15N Basic Pancreatic Trypsin Inhibitor (BPTI), using a field strength of 800 MHz for protons, magic angle sample spinning rates of 20 kHz and proton decoupling field strengths of 140 kHz. Results from two homonuclear transfer methods, radio frequency driven dipolar recoupling and spin diffusion, were compared. Typical 13C peak line widths are 0.5 ppm, resulting in Calpha-Cbeta and Calpha-CO regions that exhibit many resolved peaks. Two-dimensional carbon-carbon correlation spectra of BPTI have sufficient resolution to identify and correlate many of the spin systems associated with the amino acids. As a result, we have been able to assign a large number of the spin systems in this protein. The agreement between shifts measured in the solid state and those in solution is typically very good, although some shifts near the ion binding sites differ by at least 1.5 ppm. These studies were conducted with approximately 0.2 to 0.4 micromol of enriched material; the sensitivity of this method is apparently adequate for other biological systems as well.