triethyltin and triphenyltin

A capillary electrophoresis (CE)-indirect UV absorbance detection method for organotin compounds is described. The five triorganotin cations, viz., trimethyltin (TMT), triethyltin (TET), tripropyltin (TPT), tributyltin (TBT) and triphenyltin (TPhT), were efficiently separated by CE in 10 min with a 5 mM acetate buffer (pH 4.5) containing 3 mM 4-aminopyridine (4-AP). 4-AP also functioned as a UV-absorbing coion for the indirect detection of these UV-transparent organotin species. Simultaneous separation of di- and triorganotins was achieved with the addition of alpha-cyclodextrin (alpha-CD) as a modifier in the electrophoresis buffer. Linearity (r > or = 0.995) of about two orders of magnitude was generally obtained. The concentration limits of detection for the organotin compounds studied were between 2 and 20 microM (as tin). The relative standard deviation (RSD) values were in the range 1.3-7.1%. The applicability of the method for the analysis of marine sediment was examined.

Topics: Calibration; Electrophoresis, Capillary; Organotin Compounds; Trialkyltin Compounds; Triethyltin Compounds; Trimethyltin Compounds; Ultraviolet Rays; Water Pollutants, Chemical

Phagocytosis and concomitant release of enzymes by rabbit polymorphonuclear leukocytes (PMNs) are inhibited by micromolar concentrations of triphenyltin and tributyltin; inhibition by triethyltin occurs at higher concentrations. Chemotactic peptide-induced exocytosis is inhibited at the same concentrations as phagocytosis. Tributyltin causes cell lysis at slightly higher concentrations as required for inhibition of phagocytosis and exocytosis. The organotin compounds have little effect on ATP level in PMNs, which makes an effect on metabolic energy providing processes unlikely. The increase of Ca2+-permeability of the plasma membrane, induced by chemotactic peptide, is inhibited by the organotin compounds. Inhibition of exocytosis by triphenyltin can be counteracted by a number of sulfhydryl compounds. The results suggest that the organotin compounds interfere with PMN function in an early phase of cell activation, where all functions have a common pathway, and where vulnerable sulfhydryl groups play a pivotal role.

Topics: Adenosine Triphosphate; Animals; Calcium; Exocytosis; Neutrophils; Organotin Compounds; Phagocytosis; Rabbits; Sulfhydryl Reagents; Trialkyltin Compounds; Triethyltin Compounds; Zymosan