A hitherto unknown pattern of pathologic gastrointestinal motility--a cause of repeated vomiting?

We report the case of a 20-year-old woman with functional vomiting who presented with symptoms of anorexia nervosa. Antroduodenal and upper jejunal perfusion manometry was performed using an eight-lumen catheter. The investigation revealed a hitherto unknown motility pattern consisting of continuous simultaneous contractions at high frequency from the antrum down to the upper jejunum. The observation suggests that this disorder was related to the patients symptomatology.

Centrifugal and roller pumps--are there differences in coagulation and fibrinolysis during and after cardiopulmonary bypass?

A number of hemostatic parameters reflecting the activation of coagulation and fibrinolysis were investigated in a prospective study of 24 patients undergoing cardiopulmonary bypass (CPB) during heart surgery. The patients were randomized to a group in which either a roller (group 1) or a centrifugal pump (group 2) was used. Blood samples were taken preoperatively, at the onset of and every 20 min during CPB, after the administration of protamine, and 4, 20, 44, and 68 h postoperatively. The groups did not differ significantly in hematocrit, fibrinogen, factor XIII, and antithrombin III. Significant differences in favor of group 2 during and after CPB were found in prothrombin fragment F1 + 2, plasmin-antiplasmin complex (PAP), thrombin-antithrombin complex (TAT), and D-dimer (F1 + 2 P < 0.01 after 80-min CPB, PAP P < 0.005 after 40-min CPB, TAT and D-dimer P < 0.05 after 100-min CPB, D-dimer and PAP P < 0.05 after protamine administration, TAT and F1 + 2 4 h after CPB). These findings indicate the activation of fibrinolysis preceding thrombin generation during cardiopulmonary bypass. In addition, we conclude that centrifugal blood pumping is beneficial in avoiding excessive activation of both coagulation and fibrinolysis.

Phospholipase A activity in Pseudomonas aeruginosa.

Our study describes the production, purification and properties of an enzyme from Pseudomonas aeruginosa displaying the properties of phospholipase A. Maximal amounts of enzyme could be detected in the culture supernatant when the bacterium was grown for 3 to 5 days at 37 degrees C in stirred flask cultures containing brain heart infusion. The enzyme was purified by polyethylenimine precipitation and ammonium sulfate precipitation followed by gel filtration. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the enzyme preparation exhibited two bands with molecular weights of 13.5 and 60 kD, respectively. Correspondingly, two peaks of the same molecular weight could be demonstrated by high performance size exclusion chromatography. The activity toward the sn-2 ester binding of phospholipids was characterized and found to be highest towards phosphatidylcholine. Enzymatic activity was not influenced by the addition of calcium or EDTA while magnesium and strontium caused a decrease of activity. The lyophilized enzyme was found to be stable when stored at -70 degrees C and most active at pH 8.0.