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Sorption ability of the chitosan-modified natural zeolite for Pb2+, Cd2+, and Cu2+ cations was investigated. The influence of time and concentration of heavy metals on their sorption from concentrated (85% H3PO4) phosphoric acid was determined. At 20 and 40 min of sorption curves, there are a number of maxima probably due to desorption of cations from the sorbent into the acid. According to the results, sorption of the modified zeolite for lead cation is the least in the whole interval of time. In the case of equal concentrations of all cations (CPb=CCd=CCu), sorption of lead, cadmium, and copper was 94.81-95.09%, 96.55-97.50%, and 97.53-98.14%, respectively. Sorption curves in the case of equal Pb2+ and Cd2+, but higher concentrations of Cu2+, are the same for all cations. Sorption of cadmium varies from 95.48% to 97.55%. Copper and lead sorbed in a less amount, in the case of (CPb =CCdCu), their sorption in 10 min was 95.42% and 97.55%, respectively. As in the case of equal concentrations of all cations (CPb=CCd=CCu), the sorptions of copper, cadmium, and lead were (92.09-96.93%), (92.13-95.37%), and (91.35-94.45%), respectively, in the case of (CPb =CCuCd). Physico-chemical methods of analysis are as follows: Fourier transform infrared spectroscopy, scanning electron microscopy, x-ray powder diffraction patterns, and Brunauer-Emmett-Teller have shown that natural zeolite is activated without destroying the structure and adsorbs lead, as well as cadmium and copper cations. [ABSTRACT FROM AUTHOR]

A letter to the editor is presented about the use of recombinant factor VIIa as effective treatment modality in a patient with severe hemophilia A with high-titre inhibitors undergoing hip replacement surgery.

Presents a study on sequence specific peptidomimetic molecules inhibitors of a protein-protein interaction at the helix 1 level of c-Myc. D-amino acids found to be necessary for antiproliferative activity; Manner in which the Myc/Max heterodimer conformation was disturbed; Type of molecule that has the potential of a more selective docking at the level of a protein-protein interaction.