Determination of Diffusion Kinetics of Ketamine in Brain Tissue: Implications for Mechanistic Studies of Drug Actions.

Ketamine has been in use for over 50 years as a general anesthetic, acting primarily through blockade of -methyl-D-aspartate receptors in the brain. Recent studies have demonstrated that ketamine also acts as a potent and rapid-acting antidepressant when administered at sub-anesthetic doses. However, the precise mechanism behind this effect remains unclear.

[Synthesis of benzimidazole derivatives by amino acid action on ortho-phenylenediamine, variously substituted in positions 4 and 5].

As part of the synthesis of the benzimidazole derivative heterocyclique system, we are interested in studying the condensation of the o-phenylenediamines with amino-acids such as aspartic acid, serine and histidine. The interest that these present is based mainly on their pharmacological properties. They have, in fact anti-inflammatory, antidepressive, antibacterial and antihistamine properties.

High resolution analysis of protein phosphorylation using capillary isoelectric focusing - electrospray ionization - mass spectrometry.

On-line capillary isoelectric focusing (CIEF)-electrospray ionization - mass spectrometry (ESI-MS) as a two-dimensional separation system is employed for high resolution analysis of ovalbumin phosphorylation. On the basis of their differences in isoelectric point (pI), the mono- and diphosphoovalbumins are separated and resolved in CIEF. The focused protein zones of mono- and diphosphoovalbumins are eluted by combining gravity with cathodic mobilization.

Monitoring protein refolding induced by disulfide formation using capillary isoelectric focusing-electrospray ionization mass spectrometry.

Rapid growth in the biotechnology industry has led to a dramatic increase in attention to the protein folding problem. Understanding protein-folding pathways is essential to the production of biopharmaceuticals since commercial production of recombinant proteins often requires a protein-refolding process for recovery of high yields. Protein folding coupled to the formation of disulfide bonds presents one of the simplest approaches to studying folding intermediates.

Two-dimensional analysis of recombinant E. coli proteins using capillary isoelectric focusing electrospray ionization mass spectrometry.

On-line combination of capillary isoelectric focusing with electrospray ionization mass spectrometry is applied for a two-dimensional analysis of Escherichia coli proteins. The proteins are focused and cathodically mobilized in a polyacrylamide coated capillary. At the end of the capillary, various protein zones are analyzed by mass spectrometry coupled through an electrospray interface.