1995
DOI: 10.1016/0040-6031(95)02402-n
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The effects of scan rate and protein concentration on DSC thermograms of bovine superoxide dismutase

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Cited by 23 publications
(15 citation statements)
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“…Our estimation gives the overall average activation energy for HbA 0 equal 289 T kJ M À 1 (69 kcal M À 1 ). This value falls into the range 56-87 kcal M À 1 determined by Grasso et al [18] on the base of the procedure of Olsen and optical measurements modified by haemoglobin stabilisers.…”
Section: Two-state Kinetic Modelmentioning
confidence: 98%
“…Our estimation gives the overall average activation energy for HbA 0 equal 289 T kJ M À 1 (69 kcal M À 1 ). This value falls into the range 56-87 kcal M À 1 determined by Grasso et al [18] on the base of the procedure of Olsen and optical measurements modified by haemoglobin stabilisers.…”
Section: Two-state Kinetic Modelmentioning
confidence: 98%
“…The effect of pH variations on the thermal stability of IDE was also investigated by CD at different temperatures. This technique has the advantage of a lower usage of sample if compared to Differential Scanning Calorimetry [47,48]. The melting temperature values (Table 1) were determined from the CD melting profiles for IDE monitored at 222 nm with a heating rate of 1°C/min (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Therefore, when an irreversible process occurs, the kind of information that can be obtained from calorimetric experiments depends on each particular situation [41]. According to this, we have analyzed, in the irreversible denaturation of xylanase, the effect of the scan rate on the apparent T m .…”
Section: Resultsmentioning
confidence: 99%
“…A well-known test to determine the molecularity of the reaction, that is, whether only monomers are taking part in the unfolding process or whether oligomers are also present, is to check if the T m changes as the protein concentration increases. If this is the case, the calorimetric data obtained at several protein concentrations must be fit to (5) [40, 41]. Results depicted in Figure 5(c) show a linear dependence of ln[protein] on T m (0.4 and 0.56 mg · mL −1 , reversible process) and on apparent T m (0.8 and 1.1 mg · mL −1 , irreversible process).…”
Section: Resultsmentioning
confidence: 99%