Sarcosine and sorbitol at 10-30% (w/w) stabilized haemoglobin from human erythrocytes to thermal denaturation. At 65 degrees C, the protein's half life was increased from 0.85 to 50 min in 30% sarcosine and to 24 min in 30% sorbitol. A kinetic analysis based on the Lumry-Eyring mechanism of inactivation showed that the denaturation process can be described by a second-order rate expression with an apparent activation energy ranging from 56 to 87 kcal mol(-1).
Thermal stability of human haemoglobin in the presence of sarcosine and sorbitol / R., Di Domenico; Lavecchia, Roberto. - In: BIOTECHNOLOGY LETTERS. - ISSN 0141-5492. - 22:5(2000), pp. 335-339. [10.1023/a:1005665031667]
Thermal stability of human haemoglobin in the presence of sarcosine and sorbitol
LAVECCHIA, Roberto
2000
Abstract
Sarcosine and sorbitol at 10-30% (w/w) stabilized haemoglobin from human erythrocytes to thermal denaturation. At 65 degrees C, the protein's half life was increased from 0.85 to 50 min in 30% sarcosine and to 24 min in 30% sorbitol. A kinetic analysis based on the Lumry-Eyring mechanism of inactivation showed that the denaturation process can be described by a second-order rate expression with an apparent activation energy ranging from 56 to 87 kcal mol(-1).I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
