Biomedical subjects

Marcelo Farina

Publications and source records attributed to Marcelo Farina.

21 records · Page 2Linked to original sources

PubMed2003

Increase in serum S100B protein level after a swimming race.

Physical activity has been shown to be a beneficial stimulus to the central and peripheral nervous systems. The S100B is a cytokine physiologically produced and released predominantly by astrocytes on the central nervous system (CNS). In order to study the possible influence of a nonimpact exercise on S100B serum levels, we measured this protein serum level after a 7,600-meter swimming race. We observed an increase in S100B levels in athletes post-race compared with their baseline values, pointing to a potential acute influence of physical exercise on serum S100B levels not related with CNS injury. We discuss this result and emphasize the possible central and peripheral origins of S100B serum levels.

Adolescent↗

PubMed2002

One-step liquid-liquid extraction of cocaine from urine samples for gas chromatographic analysis.

An improved technique for cocaine extraction from urine samples for gas chromatographic (GC) analysis is described. Employing a simple liquid-liquid extraction (LLE) of cocaine with a mixture of ethyl ether:isopropanol (9:1) the method presents a mean recovery of 74.49%. Limit of detection (LOD) and limit of quantification (LOQ) were 5 and 20 ng/ml, respectively. The method is highly precise (coefficient of variation (CV) <8%) and linear from 20 to 2000 ng/ml. It can he applied to detect the presence of cocaine in urine as a marker of its recent use in drug abuse treatment protocols.

Chromatography, Gas↗

PubMed2002

Delta-aminolevulinate dehydratase inhibition by phenyl selenoacetylene: effect of reaction with hydrogen peroxide.

The effect of phenyl selenoacetylene and its selenoxide on delta-aminolevulinate dehydratase from liver of adult rats (mammalian source) and from cucumber leaves (plant source) was investigated. In vivo, selenides can be oxidized to selenoxides by flavin-containing monooxygenases and selenoxides can regenerate selenides by thiol oxidation. The compound phenyl selenoacetylene was converted to selenoxides by reaction with hydrogen peroxide. Phenyl selenoacetylene inhibited mammalian and plant delta-aminolevulinate dehydratase with an IC50 about 250 microM and >400 microM, respectively. Its selenoxide inhibited the enzyme more strongly, with IC50 values of 45 microM and 100 microM for the mammalian and plant source, respectively. The selenoxide inhibitory action was antagonized by dithiothreitol suggesting the involvement of -SH groups. Moreover, delta-aminolevulinate dehydratase from a plant source was inhibited by the selenoxide, suggesting a possible involvement of -SH groups located at a site distinct from the region implicated in Zn2+ binding in mammalian delta-aminolevulinate dehydratase. The results of the present study suggest that (i) delta-aminolevulinate dehydratase is a potential molecular target for phenyl selenoacetylene, due to the oxidation of enzyme sulfhydryl groups, and that (ii) the monooxygenation of this selenocompound, which in vivo could be possibly mediated by flavin-containing monooxigenases, increases its inhibitory effect.

Acetylene↗