We characterize linear maps on von Neumann algebras which leave every unital subalgebra invariant. We use this characterization to determine linear maps which respect unitary CONJUGATION, answering a question of M. S.Moslehian.

Introduction: [ 99m Tc]Tc-MAG3 is one of the routine renal radiopharmaceuticals being used in nuclear medicine centers, throughout the world. This study investigated the synthesis and 99m Tc-labeling of MAG3, as well as the synthesis of the S-acetyl-MAG3-NHS complexing agent, which was used for labeling bovine serum albumin (BSA) as a protein model using technetium-99m. Methods: S-acetyl-MAG3 was prepared by the reaction of S-acetyl thioglycolic acid and triglycine. It was also activated to its N-hydroxysuccinimide counterpart which was used for preparation of biomolecule conjugates. All compounds and intermediates were characterized by 1H NMR and LC/Mass spectroscopy. Labeling of MAG3 with 99m-technetium was also well performed. The radiochemical purity and stability of labeled products was done by thin-layer chromatography. Also, biodistribution studies in mice was performed. Results: The spectroscopic results confirmed the structure of compounds. The stability of [99mTc]Tc-MAG3 and [99mTc]Tc-MAG3-BSA was determined over 24h. It was found to drop from 90% to 60% and 99% to 80%, respectively. There was no difference between serum and buffer results. Biodistribution studies for [ 99m Tc]Tc-MAG3 confirmed renal excretion with injected dose per gram (%ID/g) kidney of 41. 28 ±,4. 70, 45. 63 ±,6. 36 and 12. 22 ±,2. 83 after 1, 4 and 24h respectively. Conclusion: In this work, the rigorous purification processes were simplified through adjustment of molar ratios of reactants and the crude product obtained with higher yield was directly used for 99m Tc labeling. The prepared labeled biomolecules conjugates showed acceptable radiochemical purity and stability. MAG3 was applicable for renal imaging according to biodistribution results.

Background: Staphylococcal protein A (SPA) is a cell wall component of Staphylococcus aureus that binds to different IgG subclasses of human and several animal species. This bacterial protein can be used as an antibody detector in various immunological assays or as an isolation reagent for the purification of antibody molecules via immuno-chromatography procedures.Objectives: Molecular cloning and expression of SPA followed by the purification and CONJUGATION of the recombinant protein to peroxidase enzyme.Material and Methods: Encoding DNA fragment of SPA was amplified and inserted into a prokaryotic plasmid vector for the expression of recombinant SPA fused to a maltose binding protein (MBP). The recombinant protein was purified using amylose resin column chromatography and conjugated to horseradish peroxidase (HRP) enzyme. Finally, the reactivity of the recombinant SPA was examined against human IgG molecules in ELISA.Results: The results indicated that the recombinant peroxidase-conjugated SPA has a good recognition capacity for human IgG molecules and it was able to produce significant OD values after reacting with human IgG molecules at a concentration up to 0.06mg.well-1.Conclusions: This recombinant protein can be very useful in all research laboratories and may decrease some of the expenses, e.g. those for preparing conjugated anti-antibodies.