Preparation and structural characterization of (Me(3)SiNSN)(2)Se, a new synthon for sulfur-selenium nitrides.

The reaction of (Me(3)SiN)(2)S with SeCl(2) (2:1 ratio) in CH(2)Cl(2) at -70 degrees C provides a route to the novel mixed selenium-sulfur-nitrogen compound (Me(3)SiNSN)(2)Se (1). Crystals of 1 are monoclinic and belong the space group P2(1)/c, with a = 7.236(1) A, b = 19.

Proteolysis and fusion of low density lipoprotein particles strengthen their binding to human aortic proteoglycans.

Lipid droplets resembling those seen in the extracellular space of the arterial intima were generated in vitro when granule proteases of rat serosal mast cells degraded the apolipoprotein B-100 (apoB-100) component of granule-bound low density lipoprotein (LDL), and the particles fused on the granule surface (Paanenen, K., and Kovanen, P. T.

Proteolysis and fusion of low density lipoprotein particles independently strengthen their binding to exocytosed mast cell granules.

Contact between low density lipoproteins (LDL) and exocytosed mast cell granules, the "granule remnants," leads to binding of LDL to the granule remnants via ionic interactions between the apolipoprotein B-100 (apoB-100) component of LDL and the heparin proteoglycan component of the granule remnants. Upon incubation at 37 degrees C, the heparin proteoglycan-bound apoB-100 is progressively proteolyzed by remnant chymase and carboxypeptidase A, which are also bound to the heparin proteoglycans. Thereupon, the LDL particles fuse, and their binding to the granule remnants strengthens, as defined by the decreased ability of NaCl to release LDL from the remnants.

Characterization of antigenic epitopes of potato virus Y.

Immunochemical analysis of overlapping synthetic hexapeptides covering the entire length of the coat protein of potato virus Y (PVY) revealed immunodominant regions both at the N-terminal and at the C-terminal end of the coat protein. Immunization of rabbits with synthetic peptides representing N- and C-terminal regions of the coat protein resulted in production of antibodies that reacted with PVY. Antigenicity of PVY peptides was found to correlate with predicted beta turns, with hydrophilicity and with predicted chain flexibility.