Aquaporin-1 acts as an O channel. The permeability of human and mouse red cell membranes for oxygen.

It has been demonstrated that aquaporin-1 (AQP1), one of the most abundant red cell membrane proteins, constitutes a functionally important channel for CO in red cell membranes. We ask here, whether AQP1 and other gas channel proteins play a role also in red cell oxygen transport. We use a stopped-flow technique to: ) compare the oxygen permeability, [Formula: see text], of AQP1-deficient (Colton Null) with that of normal human red cell membranes, ) compare the [Formula: see text] of with that of normal mouse red cells, ) study the effect of the gas channel inhibitor 4,4'-diisothiocyanato-2,2'-stilbenedisulfonate (DIDS) on [Formula: see text] of human and mouse red cells, and ) investigate all three effects at various temperatures between 7 and 37°C, because O transfer across channels and across membrane lipids may depend differently on temperature.

Population structure of Pneumocystis jirovecii isolated from immunodeficiency virus-positive patients.

Pneumocystis jirovecii pneumonia (PcP) is an important opportunistic infection among immunocompromised patients. Genetic characterization of P. jirovecii isolated from HIV-positive patients, based on identification of multiple nucleotide sequences at eight distinct loci, was achieved by using PCR with DNA sequencing and RFLP.