Temperature control hemoglobin

The stability of hemoglobin In a freshly prepared red cell hemolysate at temperatures varying between 50 and 70 Is distinctly less than that of a normal control. The unstable variant will also show decreased stability at 37 In the presence of the Isopropanol-trls buffer, pH 7.4. 

AmB formulations were dispersed in phosphate-buffered saline (PBS) at different concentrations (0.1 lOOpg/mL) and incubated for five minutes at 37°C. Freshly isolated human erythrocytes were then added to a final hematocrit of 2% and incubated at the same temperature for 30 minutes. After centrifugation, the supernatant was removed and the RBC pellet was lysed with sterile water. The hemoglobin remaining in the pellet was estimated from its absorption at 560 nm recorded with a spectrophotometer. The percentage hemolysis was calculated from the difference between the hemoglobin remaining in the test samples and the control incubated with PBS alone. 

Fig. 11 Effect of specific inhibitors of the respiratory chain on the nitrite reductase activity of rat liver mitochondria. Mitochondria were incubated with nitrite for 2 h under argon in the presence of succinate or glutamate/malate (Glu/Mal). Nitric monoxide derived from nitrite was trapped with hemoglobin. The concentration of NO-hemoglobin complexes was measured using low temperature ESR spectroscopy. Other details are described in Kozlov et al. [46]. CON control, ROT rotenone, TTFA thenoyltrifluoroacetone, MYX myxothiazol, AA antimycin A...

Figure 4.111 Separation of hemoglobin A2 control variants on ProSwift WCX-IS. Column dimension 50 mm x 1 mm i.d. column temperature 30 °C eluent (A) 10 mmol/L sodium phosphate-I-2 mmol/L KCN (pH 6) and (B)...

In addition to pH-responsiveness, the behavior of polymer brushes may also be altered by temperature. For instance, electrochemistry-induced radical polymerization was used to fabricate a PNIPAAm bmsh [67]. The authors used this PNIPAAm brush in conjunction with ITO to create electrically heated electrodes (H Es). Altered HEs exhibited rapid temperature increases upon heating and this temperature enhancement was reversible. The control and release properties of the HE system were then assessed by means of the model protein hemoglobin. Hemoglobin diluted in phosphate-buffered sahne was exposed to the bmsh at 20 °C when it was in the expanding state. Upon a temperature change above the brush LCST, the brush transitioned to the shrunken state, capturing the hemoglobin molecules. 

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