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 degrees C the enzyme was found to be very stable, whereas between 60 and 65 degrees 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. Study holds ProTherm entries: 10121, 10122 Extra Details: carbonic anhydrase; thermal denaturation; conformational stability;,bovine erythrocytes
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:39 p.m.
|Number of data points||3|
|Proteins||Carbonic anhydrase 2 ; Carbonic anhydrase 2|
|Assays/Quantities/Protocols||Experimental Assay: dG ; Experimental Assay: dCp ; Experimental Assay: Tm|
|Libraries||Mutations for sequence A:MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK/K:QVQLVESGGGSVQAGGSLRLSCAASGYTVSTYCMGWFRQAPGKEREGVATILGGSTYYGDSVKGRFTISQDNAKNTVYLQMNSLKPEDTAIYYCAGSTVASTGWCSRLRPYDYHYRGQGTQVTVSS|