A differential scanning calorimetric study of β-lactoglobulin and vitamin D3 complexes

2012 ◽  
Vol 110 (1) ◽  
pp. 473-477 ◽  
Author(s):  
Agata Górska ◽  
Ewa Ostrowska-Ligęza ◽  
Karolina Szulc ◽  
Magdalena Wirkowska
Keyword(s):  
Vitamin D3 ◽  
Differential Scanning Calorimetric ◽  
Calorimetric Study ◽  
Β Lactoglobulin

scholarly journals Differential Scanning Calorimetric Study of Different Genetic Variants of β-Lactoglobulin

1991 ◽  
Vol 74 (8) ◽  
pp. 2416-2422 ◽  
Author(s):  
Gilbert Idolo Imafidon ◽  
K.F. Ng-Kwai-Hang ◽  
V.R. Harwalkar ◽  
C.-Y. Ma
Keyword(s):  
Genetic Variants ◽  
Differential Scanning Calorimetric ◽  
Calorimetric Study ◽  
Β Lactoglobulin

A differential scanning calorimetric study of the thermal behaviour of bovine β-lactoglobulin at temperatures up to 160 °C

1981 ◽  
Vol 48 (2) ◽  
pp. 293-302 ◽  
Author(s):  
Jacob N. de Wit ◽  
Gijsbert Klarenbeek
Keyword(s):  
Thermal Behaviour ◽  
Conformational Changes ◽  
Temperature Shift ◽  
Differential Scanning Calorimetric ◽  
Calorimetric Study ◽  
Scanning Calorimetry ◽  
Maximum Heat ◽  
Β Lactoglobulin ◽  
Endothermal Peak ◽  
Dsc Curves

SummaryThe thermal behaviour of β-lactoglobulin was studied by differential scanning calorimetry (DSC) in the temperature range 40–160 °C. The DSC curves revealed, in addition to the usually observed denaturation peak near 80 °C, a distinct endothermal peak between 130 and 150 °C. When the pH was increased from 6·5, the area under the peak near 80 °C (denaturation heat) decreased significantly, whereas the peak area near 140 °C increased. The temperature of maximum heat absorption in the peaks near both 80 and 140 °C gradually increased as the pH decreased. Addition of sugars and variation of the heating rate both caused a temperature shift of the endothermal heat effect at 140 °C, similar to that at 80 °C. No peak near 140 °C was observed when β-mercapto-ethanol was added to the β-lactoglobulin solution before scanning. The origin and nature of the high temperature denaturation peak is discussed in terms of conformational changes of the protein.

A comparative differential scanning calorimetric study of tobacco mosaic virus and of its coat protein ts mutant

FEBS Letters ◽  
1998 ◽  
Vol 433 (3) ◽  
pp. 307-311 ◽  
Author(s):  
V.N. Orlov ◽  
S.V. Kust ◽  
P.V. Kalmykov ◽  
V.P. Krivosheev ◽  
E.N. Dobrov ◽  
...  
Keyword(s):  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Differential Scanning Calorimetric ◽  
Calorimetric Study ◽  
Ts Mutant

Differential scanning calorimetric study of the thermal unfolding of the motor domain fragments of Dictyostelium discoideum myosin II

1998 ◽  
Vol 251 (1-2) ◽  
pp. 275-280 ◽  
Author(s):  
Dmitrii I. Levitsky ◽  
Michael A. Ponomarev ◽  
Michael A. Geeves ◽  
Valery L. Shnyrov ◽  
Dietmar J. Manstein
Keyword(s):  
Dictyostelium Discoideum ◽  
Myosin Ii ◽  
Motor Domain ◽  
Thermal Unfolding ◽  
Differential Scanning Calorimetric ◽  
Calorimetric Study
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