PubMed · 13075599
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
G MATHE. 1953-06-11. [Hemolysis tests].. https://pubmed.ncbi.nlm.nih.gov/13075599/
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Six human isolates of group B streptococci (GBS) were cultured on blood agar anaerobically at 37 degrees C for 18 h and then at 4 degrees C for 6 h and reincubated anaerobically at 37 degrees C for 6 h. Three of the strains showed a marked enlargement of the hemolysis zone compared with that obtained after hot-only (37 degrees C for 18 h) or hot-cold (37 degrees C for 18 h and then 4 degrees C for 6 h) treatment. Subsequent broth culture experiments revealed that enhanced hemolytic activity due to hot-cold-hot treatment was observed in all 6 GBS strains when cultured in the presence of starch.
Explore the source record for details and available documents.
Surface tension measurements were employed to monitor the erythrocyte hemolysis process induced by surfactants. Two types of surfactants were used: the cationic surfactant DTAB and the anionic surfactant SDS. During DTAB-induced hemolysis, the changes in surface tension clearly demonstrate three stages. The first stage is characterized by surface tension increase, which is explained by surfactant removal from the suspending solution, due to adsorption onto cell membranes. In the second stage, surface tension remains constant, implying that equilibrium is attained between the membrane-bound surfactant and the surfactant in solution. The third stage is characterized by surface tension decrease that begins simultaneously with measurable cell-interior release, and lasts until hemolysis is completed. With SDS-induced hemolysis, the same three stages are observed at a low concentration; however, fluctuational increase in surface tension is obtained for higher concentrations. The latter is explained by additional adsorption of surfactant to solubilized membrane fragments.