Unfolding mechanism and stability of immobilized papain

Autor: E. Battistel, G. Rialdi
Rok vydání: 1996
Předmět:
Zdroj: Journal of Thermal Analysis. 47:17-25
ISSN: 1572-8943
0368-4466
DOI: 10.1007/bf01982682
Popis: The thermal stability of papain in free solution or immobilized on CPC-silica has been investigated by DSC. At neutralpH, in both conditions, the protein undergoes a thermal transition which corresponds to the sum of two transitions associated with the unfolding of the two domains of the protein. At lowpH, in the case of immobilized papain, only one transition is observed.
Databáze: OpenAIRE
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