Literature DB >> 1959599

Thermal denaturation of erythrocyte carbonic anhydrase.

R Lavecchia1, M Zugaro.   

Abstract

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.

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Year:  1991        PMID: 1959599     DOI: 10.1016/0014-5793(91)80858-z

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

Review 1.  Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.

Authors:  Vijay M Krishnamurthy; George K Kaufman; Adam R Urbach; Irina Gitlin; Katherine L Gudiksen; Douglas B Weibel; George M Whitesides
Journal:  Chem Rev       Date:  2008-03       Impact factor: 60.622

2.  Exploring local flexibility/rigidity in psychrophilic and mesophilic carbonic anhydrases.

Authors:  R Chiuri; G Maiorano; A Rizzello; L L del Mercato; R Cingolani; R Rinaldi; M Maffia; P P Pompa
Journal:  Biophys J       Date:  2009-02-18       Impact factor: 4.033

3.  Protein-caged zinc porphyrin as a carbonic anhydrase mimic for carbon dioxide capture.

Authors:  Haixia Chi; Han Chen; Kai Gong; Xiaoqiang Wang; Youming Zhang
Journal:  Sci Rep       Date:  2020-11-11       Impact factor: 4.379

  3 in total

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