Enthalpy–entropy compensation in the denaturation of proteins of bovine masseter and cutaneous trunci

Meat Science ◽  
2022 ◽  
Vol 184 ◽  
pp. 108688
Author(s):  
Jonghoon Kang ◽  
Karla A. Solis Rueda
Keyword(s):  
Denaturation Of Proteins

scholarly journals On the Structural Stability and Solvent Denaturation of Proteins

1971 ◽  
Vol 246 (20) ◽  
pp. 6370
Author(s):  
Theodore T. Herskovits ◽  
Barbara Gadegbeku ◽  
Helen Jaillet
Keyword(s):  
Structural Stability ◽  
Denaturation Of Proteins

scholarly journals THE DENATURATION OF PROTEINS AND ITS APPARENT REVERSAL

1942 ◽  
Vol 144 (1) ◽  
pp. 259-264 ◽  
Author(s):  
Frederick Bernheim ◽  
Hans Neurath ◽  
John O. Erickson
Keyword(s):  
Denaturation Of Proteins

Denaturation of proteins-60 years on

1996 ◽  
Vol 24 (4) ◽  
pp. 213-214
Author(s):  
Keith Manchester
Keyword(s):  
Denaturation Of Proteins

scholarly journals Mechanism of hydration of urea and guanidium ion: A model study of denaturation of proteins

1998 ◽  
Vol 70 (3) ◽  
pp. 659-664 ◽  
Author(s):  
Fateh S. Nandel ◽  
Rajnish Verma ◽  
Balvinder Singh ◽  
Dharam V. S. Jain
Keyword(s):  
Model Study ◽  
Denaturation Of Proteins

scholarly journals Chicken Intestinal Alkaline Phosphatase

1960 ◽  
Vol 43 (6) ◽  
pp. 1149-1169 ◽  
Author(s):  
M. Kunitz
Keyword(s):  
Alkaline Phosphatase ◽  
Zinc Ions ◽  
Magnesium Ions ◽  
Intestinal Alkaline Phosphatase ◽  
Reversible Inactivation ◽  
Higher Temperature ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Zn Ions ◽  
Denaturation Of Proteins

Purified chicken intestinal alkaline phosphatase is active at pH 8 to 9, but becomes rapidly inactivated with change of pH to 6 or less. Also, a solution of the inactivated enzyme at pH 4.5 rapidly regains its activity at pH 8. In the range of pH 6 to 8 a solution of purified alkaline phosphatase consists of a mixture of active and inactive enzyme in equilibrium with each other. The rate of inactivation at lower pH and of reactivation at higher pH increases with increase in temperature. Also, the activity at equilibrium in the range of pH 6 to 8 increases with temperature so that a solution equilibrated at higher temperature loses part of its activity on cooling, and vice versa, a rise in temperature shifts the equilibrium toward higher activity. The kinetics of inactivation of the enzyme at lower pH and the reactivation at higher pH is that of a unimolecular reaction. The thermodynamic values for the heat and entropy of the reversible inactivation and reactivation of the enzyme are considerably lower than those observed for the reversible denaturation of proteins. The inactivated enzyme at pH 4 to 6 is rapidly reactivated on addition of Zn ions even at pH 4 to 6. However, zinc ions are unable to replace magnesium ions as cocatalysts for the enzymatic hydrolysis of organic phosphates by alkaline phosphatase.

A calorimetric approach to the kinetics of the irreversible thermal denaturation of proteins

1992 ◽  
Vol 199 ◽  
pp. 147-157 ◽  
Author(s):  
María L. Galisteo ◽  
Francisco Conejero-Lara ◽  
Josefa Núñez ◽  
Jose M. Sánchez-Ruiz ◽  
Pedro L. Mateo
Keyword(s):  
Thermal Denaturation ◽  
Kinetics Of ◽  
Denaturation Of Proteins
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