Characterization of structure and diffusion behaviour of Ca-alginate beads prepared with external or internal calcium sources.

Ca-alginate beads were prepared with either external or internal calcium sources. The structures of both beads were investigated with the aid of scanning electron microscopy (SEM) and confocal microscopy. It was shown that the beads with internal calcium source had a looser structure and bigger pore size than those with external calcium source. The attempts to interpret the difference were carried out by determining the Ca content within the beads at various times, which indicated that it was the different gelation mechanisms that caused the difference of structures of both beads. Furthermore, it was also found that the diffusion rate of haemoglobin (Hb) within the beads with an internal calcium source was faster than that of the beads with an external one, which was consistent with the observation of their structures.

Bidentate Lewis base adducts of methyltrioxorhenium(VII) and their application in catalytic epoxidation.

Methyltrioxorhenium(VII) (MTO) forms octahedral adducts with bidentate Lewis bases. These complexes were isolated and fully characterized, including X-ray crystallography. The compounds display distorted octahedral geometry in the solid state with a tendency of disorder concerning the Re central atom. At elevated temperatures, they undergo rapid ligand-exchange reactions in solution. The ease of this ligand exchange depends mainly on the Lewis basicity of the ligand. The more Lewis basic the ligand is, the stronger the metal-ligand interaction is, as can be shown by NMR spectroscopy. All examined complexes are temperature stable but quite sensitive to light and moisture. In the presence of H(2)O(2), the complexes form very active and highly selective epoxidation catalysts. Peroxo complexes are generated, and at least one of the Re-N interactions is cleaved during this process. Total ligand dissociation only occurs in the case of very weakly coordinating bidentate ligands. The peroxo complexes of the MTO Lewis base adducts are, in general, more sensitive to water than MTO itself.

Genetic determinants of serum prostate-specific antigen levels in healthy men from a multiethnic cohort.

We recently reported an association between prostate cancer risk and polymorphisms in the prostate-specific antigen (PSA) and androgen receptor (AR) genes. The purpose of this study is to test whether these two polymorphisms, AR CAG and PSA ARE1, influence serum PSA levels in healthy men. Serum PSA and the two genotypes were assayed for 420 healthy men from a multiethnic cohort, and regression models were fit to estimate the effects of AR CAG genotype and PSA ARE1 genotype on serum PSA levels. Predicted serum PSA decreased 3.5% with each additional AR CAG repeat decile (P = 0.01). Serum PSA was also associated with PSA ARE1 genotype, with PSA levels higher among men with the PSA AA genotype compared with men with the AG or GG genotypes (P = 0.02). The relationship between serum PSA level and AR CAG length differed according to PSA genotype (P = 0.049): for genotype GG, the slope was not significantly different from zero (P = 0.74); for genotype AG, serum PSA increased 4.5% with each decrease of one CAG repeat decile (P = 0.03); for genotype AA, serum PSA increased 7% with each decrease of one CAG repeat decile (P = 0.02). These results indicate that in healthy men, genetic variants in the PSA and AR genes contribute to variation in serum PSA levels. Men with the PSA AA genotype and short AR CAG alleles have, on average, higher serum PSA levels.