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A systematic quantification of carbonic anhydrase transcripts in the mouse digestive system

Pei-wen Pan*, Alejandra Rodriguez and Seppo Parkkila

BMC Molecular Biology 2007, 8:22 doi:10.1186/1471-2199-8-22

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Modification of carbonic anhydrase II with acetaldehyde, the first metabolite of ethanol, leads to decreased enzyme activity

Fatemeh Bootorabi, Janne Jänis, Jarkko Valjakka, Sari Isoniemi, Pirjo Vainiotalo, Daniela Vullo, Claudiu T Supuran, Abdul Waheed, William S Sly, Onni Niemelä, Seppo Parkkila BMC Biochemistry 2008, 9:32 (27 November 2008)

Abstract | Full text | PDF | PubMed |  Editor’s summary

Acetaldehyde, a metabolite of ethanol, forms a Schiff base with one of the amino groups of carbonic anhydrase II, and its inhibition of this enzyme by covalent modification may help explain the toxicity of ethanol in human tissues.

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