Search

We present a thermodynamic analysis of the sustainable use of resources in the province of Modena, focusing the attention on the district of Sassuolo. The methodology that is used is the emergy evaluation. The analysis shows that the Sassuolo district represents the peak of non-sustainability of the whole area, with a huge consumption of non-renewable primary resources, both imported and local. The role of the ceramic tile industry is relevant in the consumption of energy and materials. Different types of factories for ceramics production are compared, representing a good sample of different methods of production. Emergy analysis shows which of these has higher levels of sustainability with respect to the others.

The kinetic behavior of the spin label MAL-6 in the interaction with differently aged human erythrocyte membranes was evaluated by monitoring the rate of disappearance of the room temperature ESR signal due to the MAL-6 spin label added to blood after storage at 4 °C or after incubation of red cells at 37 °C in a protein-free medium. After 35 days of blood storage or 60 h of erythrocytes incubation at 37 °C the decrease of the intensity of the MAL-6 ESR spectra in respect to control samples is markedly enhanced and the correspondent kinetic constants significantly increase. Signal decay of MAL-6 is a further proof that during storage of blood under blood bank conditions or during an artificial ageing of erythrocytes at 37 °C, profound modifications occur in the human erythrocyte membrane.

Murine sex-limited protein (Slp) is an isotype of murine complement component C4 that shares 95% sequence identity with C4 as well as the intramolecular thioester necessary for C4 function but has no complement activity. Slp is nonfunctional at least in part because it is not cleaved by the activated form of complement protease C1s (C1s), which proteolytically activates C4 in the classical complement pathway. Slp is also distinct from C4 in that its expression in some mouse strains is under testosterone control. In the present studies, we used site-directed mutagenesis of C4 and expression of the mutant proteins in cultured cells to identify the amino acid substitutions in Slp that are responsible for resistance to C1s cleavage. We focused on sequence changes immediately downstream of the cleavage site in C4 because the arginine at that site is conserved in Slp, but the downstream sequences diverge substantially, with six differences in the first 7 residues followed by a 3-residue deletion in Slp. We found that a C4 mutant carrying only the 3-residue deletion is not cleaved by C1s and has essentially no hemolytic activity, whereas a mutant carrying only the six replacement changes is cleaved by C1s and has normal hemolytic activity. Both mutants have intact thioesters. A third mutant in which two acidic residues in the segment deleted in Slp were replaced by aliphatic residues is also cleaved by C1s, has an intact thioester group, and has normal hemolytic activity. These results indicate that the downstream mutations are responsible for the resistance of Slp to C1s cleavage and suggest that the length rather than the specific sequence of this segment is critical in determining susceptibility to the protease.

The crystalline 1:1:1 complexes of Cu(II), (I) and the bases (III)‐(V), the 1:1 complex of Cu(II) and (II), and the 1:1:1 complex of Cu(II), (II) and (IV) are prepared by known methods.