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Biomedical subjects

K Sekeri-Pataryas

Publications and source records attributed to K Sekeri-Pataryas.

3 recordsLinked to original sources

Radiochemical and radioimmunological data of 99Tcm-anti-CEA labelled by two diverse methods.

The aim of this study was to make a comparative evaluation of a direct and an indirect method for the labelling of anti-CEA with technetium-99m (99Tcm). With the direct method, disulphide bridges were cleaved by the use of 2-mercaptoethanol as reductant, whereas with the indirect method, the antibody was coupled to 2-iminothiolane. In both cases, a preformed intermediate chelate was used for 99Tcm exchange. The radiochemical and radiobiological behaviour of the 99Tcm-labelled species were studied. Furthermore, the influence of the labelling systems on the integrity of monoclonal antibodies, as well as the ability of 99Tcm-anti-CEA to tag onto human cancer cells, was investigated for the two labelling systems. Both methods showed a high labelling yield and resulted in immunoreactive and stable derivatives. However, detailed electrophoretical and radiochemical data, as well as the cysteine challenge trial, indicated relatively greater stability for the 2-mercaptoethanol reduction procedure.

Animals↗

Prothymosin alpha is not a nuclear polypeptide.

Using a radioimmunoassay for the NH2-terminus of prothymosin alpha, the crossreactive material was measured in subcellular fractions of calf thymus and liver. No significant amount of crossreactive material was found in the nucleus. This provides experimental evidence against a recent hypothesis, based on structural evidence, that prothymosin alpha is a nuclear polypeptide.

Animals↗

Outer membrane proteins in a carbenicillin-resistant strain of Pseudomonas aeruginosa.

The outer membrane of a clinical isolate of Pseudomonas aeruginosa sensitive to carbenicillin, and its derivative adapted to grow in the presence of carbenicillin were analysed by polyacrylamide gel electrophoresis. The lack of beta-lactamase activity showed that the resistance of the adapted strain was not due to hydrolysis of carbenicillin. The appearance of several outer membrane proteins almost exclusively in the resistant strain supports the view of altered cell envelope properties in this strain.

Bacterial Proteins↗