Robert Osterberg

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When ammonium dihydrogen phosphate is heated with urea to temperatures in the range 85–100°C, it polymerizes almost quantitatively to give polyphosphates containing, on the average, more than ten (PO3) residues. Similar experiments carried out at 72°C give polyphosphate in more than 60% yield. If a nucleoside (thymidine or 3′-deoxythymidine) is added to the(More)
Excessive fluoride (F) in drinking water should be removed, but simple, inexpensive methods of fluoride removal are not readily available. This study examines the F(-)-binding capacity of clay and clayware, especially the effect of the firing temperature on the F(-)-binding process. A series of pots were made from ordinary potter's clay and fired at(More)
The complex formation between elongation factor Tu (EF-Tu), GTP, and valyl-tRNAVal1A has been investigated in a hepes buffer of "pH" 7.4 and 0.2 M ionic strength using the small-angle neutron scattering method at concentrations of D2O where EF-Tu (42% D2O) and tRNA (71% D2O) are successively matched by the solvents. The results indicate that EF-Tu undergoes(More)
Equilibrium analysis of a model system for the in vivo reactions between penicillamine and Cu(I), the penicillamine-glutathione-Cu(I) system, indicates that in a certain concentration range the use of penicillamine as a drug will not disturb the normal Cu(I) metabolism. The equilibrium data required for this analysis were obtained by emf titrations on the(More)
Methylamine induces a conformational change of alpha 2-macroglobulin which is very similar to that obtained by proteinase reaction and binding. This was shown by small-angle X-ray scattering at 21 degrees C in 0.03 M Hepes buffer of pH 8.0 containing 0.15 M NaCl and 0.3 mM EDTA. When alpha 2-macroglobulin reacts with methylamine the side maximum virtually(More)
The interaction between human alpha 2-macroglobulin and trypsin yields a complex of two trypsin molecules and one alpha 2-macroglobulin molecule as the main product. This is indicated from small-angle X-ray titration measurements in 0.02 M Tris/HCl buffer of pH 7.40 containing 0.2 M NaCl and 5 mM EDTA. The radius of gyration for the complex was determined(More)
X-Ray scattering study of alpha 2-macroglobulin in solvents of variable electron densities (sucrose in water) shows that alpha 2-macroglobulin obeys the invariant volume hypothesis; thus, the structure of the particle is independent of the sucrose concentration of the solution. The particle structure is quantitatively described by a set of parameters such(More)