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Thermal denaturation of erythrocyte carbonic anhydrase
Author(s) -
Roberto Lavecchia,
Marco Zugaro
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80858-z
Subject(s) - carbonic anhydrase , denaturation (fissile materials) , enzyme , chemistry , thermal stability , enzyme assay , biochemistry , carbonic anhydrase ii , thermodynamics , organic chemistry , nuclear chemistry , physics
An experimental study on the thermal behaviour of erythrocyte carbonic anhydrase was carried out with the main aim to estimate the thermodynamic parameters that control the stability of the enzyme. The effects of thermal denaturation on the catalytic properties of the enzyme were also investigated. Below 60°C the enzyme was found to be very stable, whereas between 60 and 65°C a drastic decrease in the biological activity was observed. From the obtained results some considerations were made about the stabilization of the active form of the protein.