[Absorption of L-lysine diatrizoate from the gastrointestinal tract: the influence of surgery, inflammation and neoplasia]. / Resorption von L-Lysin-Diatrizoat aus dem Gastrointestinaltrakt unter dem Einfluss von Operation, Entzündung und Neoplasie.

PURPOSE: To ascertain whether the absorption of L-lysine diatrizoate, a sodium-free salt of the contrast-giving diatrizoic acid, from the gastrointestinal tract is increased by surgery, inflammation or neoplasia. MATERIAL AND METHODS: Using contrast medium containing L-lysine diatrizoate for intestinal opacification, this prospective study compared 32 radiographic examinations of the upper gastrointestinal tract with 52 radiographic examination of the lower gastrointestinal tract. In blood samples taken from the patients immediately after the radiographic examinations, the concentration of diatrizoic acid was determined by high pressure liquid chromatography. The results were correlated with sex, age, surgical history and any evidence of inflammatory or neoplastic diseases. RESULTS: The serum diatrizoic acid concentration in patients after oral administration was 3.62 (95% CI, 2.86 - 10.17) microg/ml. The titer was lower in patients who had undergone abdominal surgery than in patients without surgery. Serum diatrizoic acid concentration in patients after rectal administration was 0.30 (95% CI, 0.13 - 0.60) microg/ml. The titer was significantly higher (p < 0.05) in patients suffering from inflammatory conditions or neoplasms than in the other patients. CONCLUSION: The L-lysine salt of diatrizoic acid is absorbed in larger amounts from the upper than from the lower gastrointestinal tract. Absorption is not increased after abdominal surgery. However, inflammatory conditions and neoplasms of the large bowel increase the uptake of contrast medium from the intestine.

Properties of the F0F1 ATPase complex from Rhodospirillum rubrum chromatophores, solubilized by Triton X-100.

1. A cold-stable oligomycin-sensitive F0F1 ATPase complex from chromatophores of Rhodospirillum rubrum FR 1 was solubilized by Triton X-100 and purified by gel filtration. 2. The F0F1 complex is resolved by sodium dodecyl sulfate electrophoresis into 14 polypeptides with approximate molecular weights in the range of 58000--6800; five of these polypeptides are derived from the F1 moiety of the complex which carries the catalytic centers of the enzyme. 3. The purified F0F1 complex is homogeneous according to analytical ultracentrifugation and isoelectric focusing. 4. The molecular weight as determined by gel filtration is about 480 000 +/- 30 000. S020,w is 1.45 +/- 0.1 S and the pI is 5.4. 5. The amino acid composition of the F0F1 complex is compared with the data obtained for the F1 moiety of the enzyme. 6. Quantitative data on the sensitivity to N,N'-dicyclohexyl-carbodiimide as well as kinetic parameters, regarding substrate specificity and dependence of ATPase activity on divalent cations, are reported.

Immunological properties of membrane-bound adenosine triphosphatase: immunological identification of rutamycin-sensitive F0.F1ATPase from Micrococcus luteus ATCC 4698 established by crossed immunoelectrophoresis.

(1) F0.F1ATPase (EC 3.6.1.3) from Micrococcus luteus ATCC 4698 was solubilized from plasma membranes by the non-ionic detergent Triton X-100 in the presence of 0.05 M MgCl2. (2) The antibiotics rutamycin, Dio-9, quercetin, oligomycin, botrycidin, efrapeptin, leucinostatin, valinomycin, and venturicidin as well as N,N'-dicyclohexylcarbodiimide and dinitrophenol are potent inhibitors of F0.F1ATPase activity.(3) F0.F1ATPase activity is completely inhibited by anti-F1ATPase antibodies. The inhibition is non-competitive. (4) Crossed immunoelectrophoresis reveals a reaction of immunological identity of F0.F1ATPase and F1ATPase indicating that both enzymes have in common antigenic sites.