Human cathepsin B, the most abundant lysosomal cysteine protease, has been implicated in a variety of important physiological and pathological processes. It has been known for a long time that like other lysosomal cysteine proteases, cathepsin B becomes inactivated and undergoes irreversible denaturation at neutral or alkaline pH. However, the mechanism of this denaturation process remains most...

The denaturation of ribonuclease A, lysozyme alpha-lactalbumin, and myoglobin by urea, guanidine hydrochloride, and guanidine thiocyanate has been followed with the use of difference spectral measurements. The free energy of stabilization (delta GH2OD) has been determined by the linear extrapolation of the free energy of denaturation to zero denaturant concentration. The values of delta GH2OD a...

The structural stability of a peroxidase, a dimeric protein from palm tree Chamaerops excelsa leaves (CEP), has been characterized by high-sensitivity differential scanning calorimetry, circular dichroism and steady-state tryptophan fluorescence at pH 3. The thermally induced denaturation of CEP at this pH value is irreversible and strongly dependent upon the scan rate, suggesting that this pro...

Chemical denaturation and thermal denaturation of13-lactoglobulin A (f3 — lgA) in the absenceand presence of various concentrations sugar osmolytes and polyols were measured bymonitoring changes in the absorption coefficients at pH 2.0. It has been observed that AGD°(H20), (Gibbs free energy change in absence of denaturant at 25 °C) of f3-1gA in the presenceof 10% (w/v) Trehalose, Sucrose, Sorb...

The effect of nucleotides on the structure and thermal stability of ferricytochrome c was studied by differential scanning calorimetry. The association of cytochrome c with ATP and ADP resulted in a decrease in the denaturation temperature of cytochrome c by 7 degrees C and 4 degrees C, respectively, at pH 7.0. AMP did not change the denaturation temperature of cytochrome c at pH 7.0. The ratio...

A simple and effective device for investigating heat-induced denaturation of proteins by electrospray ionization mass spectrometry is described. Results are presented for the denaturation as a function of temperature and solution pH of bovine ubiquitin and bovine cytochrome c. These results are in concert with and extend the earlier results of LeBlanc et al. (Org. Mass Spectrom. 1991, 26, 831)....

Denaturation of Bordetella pertussis fimbrial preparations by guanidinium hydrochloride (GdnHCl) has been characterized using static light scattering, c.d., fluorescence and antibody recognition. The susceptibility of Fim2 + 3 (a mixed preparation of two fimbrial types) to GdnHCl was found to be highly dependent on pH; as the pH was increased from pH 7.2 to 10.5, the concentration of GdnHCl req...

Systematic photometric studies are presented to analyze the thermal denaturation behaviour with and without formamide of metaphase chromosome suspensions in comparison to DNA solutions. Temperature dependent hyperchromicity measurements at 256 nm and 313 nm were performed using an appropriately designed computer-controlled photometer device. Due to an upright optical axis, this allowed absorban...

human serum albumin has been used as a model protein for protein folding and ligand binding studies over many decades. due to its long life period and high concentration in plasma, hsa is highly sensitive to glycation. it is reported that 175 mg/dl glucose concentration is a threshold of kidney activity for the beginning of excretion of glucose. ph denaturation of hsa in absence and presence of...

Differential scanning calorimetric (DSC) measurements were performed on the thermal denaturation of lysozyme and lysozyme complexed with N-acetyl-D-glucosamine (GlcNAc) at pH 5.00 (acetate buffer), 4.25 and 2.25 (Gly-HCl buffer). DSC data have been analyzed to obtain denaturation temperature T(d), enthalpy of denaturation DeltaH(D), heat capacity of denaturation DeltaC(pd) and cooperativity ind...