Thoracic cavity fluid as an alternative specimen for carboxyhaemoglobin measurement in post-mortem toxicology.

Post-mortem blood is most frequently used for the measurement of carboxyhaemoglobin (COHb) in post-mortem forensic cases, when investigating suspected inhalation of carbon monoxide (CO). However, in many post-mortem cases (especially severe burns and charring deaths), adequate blood specimens are not always available for toxicological analyses. Here, the availability of an alternative specimen for COHb analysis is required. This study investigated the suitability of thoracic cavity fluid (TCF) as an alternative specimen for the measurement of COHb. TCF and comparative blood samples from fifteen potential CO toxicity cases were collected into green-top tubes (containing lithium heparin) and analysed immediately after collection using a validated method on the ABL825 FLEX Radiometer CO-oximeter. Pearson's correlation coefficient indicated a strong positive relationship between the two specimens (r = 0.975, n = 10, p < 0.001). A statistical agreement between COHb concentrations from blood and TCF was demonstrated using the Bland-Altman plot, with a slight bias of 1.54 % when blood was taken as the standard. This study found that TCF would be a suitable alternative to blood for the measurement of COHb using the ABL825 FLEX blood gas analyser.

Plasmodium falciparum Hep1 Is Required to Prevent the Self Aggregation of PfHsp70-3.

The majority of mitochondrial proteins are encoded in the nucleus and need to be imported from the cytosol into the mitochondria, and molecular chaperones play a key role in the efficient translocation and proper folding of these proteins in the matrix. One such molecular chaperone is the eukaryotic mitochondrial heat shock protein 70 (Hsp70); however, it is prone to self-aggregation and requires the presence of an essential zinc-finger protein, Hsp70-escort protein 1 (Hep1), to maintain its structure and function. PfHsp70-3, the only Hsp70 predicted to localize in the mitochondria of P. falciparum, may also rely on a Hep1 orthologue to prevent self-aggregation. In this study, we identified a putative Hep1 orthologue in P. falciparum and co-expression of PfHsp70-3 and PfHep1 enhanced the solubility of PfHsp70-3. PfHep1 suppressed the thermally induced aggregation of PfHsp70-3 but not the aggregation of malate dehydrogenase or citrate synthase, thus showing specificity for PfHsp70-3. Zinc ions were indeed essential for maintaining the function of PfHep1, as EDTA chelation abrogated its abilities to suppress the aggregation of PfHsp70-3. Soluble and functional PfHsp70-3, acquired by co-expression with PfHep-1, will facilitate the biochemical characterisation of this particular Hsp70 protein and its evaluation as a drug target for the treatment of malaria.