scholarly journals Thermodynamic studies on subunit assembly in human hemoglobin. Temperature dependence of the dimer-tetramer association constants for oxygenated and unliganded hemoglobins.

1977 ◽  
Vol 252 (1) ◽  
pp. 82-87 ◽  
Author(s):  
S H Ip ◽  
G K Ackers
Keyword(s):  
Temperature Dependence ◽  
Association Constants ◽  
Human Hemoglobin ◽  
Thermodynamic Studies ◽  
Subunit Assembly

Linkage between cooperative oxygenation and subunit assembly of cobaltous human hemoglobin

Biochemistry ◽  
1991 ◽  
Vol 30 (29) ◽  
pp. 7263-7271 ◽  
Author(s):  
Michael L. Doyle ◽  
Phil C. Speros ◽  
Vince J. LiCata ◽  
David Gingrich ◽  
Brian M. Hoffman ◽  
...  
Keyword(s):  
Human Hemoglobin ◽  
Subunit Assembly

Effects of Anions on the Ligand-Linked Subunit Assembly of Human Hemoglobin: The Mutual Effects of Cl−and Edta

Hemoglobin ◽  
1983 ◽  
Vol 7 (2) ◽  
pp. 141-157 ◽  
Author(s):  
Joelle Thillet ◽  
Amy H. Chu ◽  
Paul Romeo ◽  
Andreas Tsapis ◽  
Gary K. Ackerst
Keyword(s):  
Human Hemoglobin ◽  
Subunit Assembly

scholarly journals Thermodynamic studies on the hydrolysis of cytidine 2′:3′-phosphate by bovine pancreatic ribonuclease A. A possible effect of the change of the structure of water

1980 ◽  
Vol 189 (3) ◽  
pp. 655-657 ◽  
Author(s):  
J A Biosca ◽  
C M Cuchillo
Keyword(s):  
Temperature Dependence ◽  
Ribonuclease A ◽  
Thermodynamic Studies ◽  
Pancreatic Ribonuclease ◽  
Structure Of Water ◽  
Pancreatic Ribonuclease A ◽  
Hydrolysis Of

The temperature-dependence of the ribonuclease A-catalysed hydrolysis of cytidine 2′:3′-phosphate was studied in the range of temperatures 0–40 degrees C. A break at 4 degrees C was found both in the Arrhenius and the van't Hoff plots. It is likely that the transition observed is due to the change in the structure of water.

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