Transfer RNA binding to human serum albumin: a model for protein-RNA interaction.

Protein-RNA complexation is essential in cell biological functions. Transfer RNAs are bound to aminoacyl-tRNA synthetases for the translation of the genetic code during protein synthesis, while ribonucleoproteins bind RNA in posttranscriptional regulation of gene expression. A recent report showed the interacton of human serum albumin (HSA) with DNA duplex, in which two binding sites with strong and weak association constants were detected.

DNA interaction with human serum albumin studied by affinity capillary electrophoresis and FTIR spectroscopy.

The question addressed in this study is how does the protein-DNA complexation affect the structure and dynamics of DNA and protein in aqueous solution. We examined the interaction of calf-thymus DNA with human serum albumin (HSA) in aqueous solution at physiological conditions, using constant DNA concentration of 12.5 mM (phosphate) and various HSA contents 0.

Taxol anticancer activity and DNA binding.

The interaction of taxol with DNA has major biological importance since it is shown the presence of higher concentration of taxol in the nucleus, than in the human lung tumor cell. Therefore, in this report we examine the interaction of taxol with calf-thymus DNA in aqueous solution at physiological pH, using constant DNA concentration (25 or 1.25 mM phosphate) and various taxol/DNA (phosphate) ratios 1/200 to 1/2.

[Risk factors of intrauterine growth retardation in Congo].

A case-control study was performed between April 1st and September 30th to investigate determinants of intrauterine growth retardation (IUGR) in 3 centers in Brazzaville, Congo. Each patient group included 539 neonates. Cases were newborns with birth weight below the 10th percentile of the Leroy and Lefort curve.

Secondary structural analysis of the Na(+),K(+)-ATPase and its Na(+) (E(1)) and K(+) (E(2)) complexes by FTIR spectroscopy.

The Na(+),K(+)-ATPase is an integral membrane protein which transports sodium and potassium cations against an electrochemical gradient. The transport of Na(+) and K(+) ions is presumably connected to an oscillation of the enzyme between the two conformational states, the E(1) (Na(+)) and the E(2) (K(+)) conformations. The E(1) and E(2) states have different affinities for ligand interaction.