Biochemical characterization of a S-glutathionylated carbonic anhydrase isolated from gills of the Antarctic icefish Chionodraco hamatus
Gill cytoplasmic carbonic anhydrase of the haemoglobinless Antarctic icefish Chionodraco hamatus (Ice-CA) was directly sequenced and consists in 259 residues with an acetylated Nterminus. The molecular mass, deduced from the sequence, was 28.45 kDa, while mass spectrometry analysis of the native pro...
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ftunivsalento:oai:iris.unisalento.it:11587/300517 2024-04-21T07:50:18+00:00 Biochemical characterization of a S-glutathionylated carbonic anhydrase isolated from gills of the Antarctic icefish Chionodraco hamatus RIZZELLO, Antonia ACIERNO, Raffaele VERRI, Tiziano STORELLI, Carlo MAFFIA, Michele M. A. CIARDIELLO V. CARRATORE G. DI PRISCO Rizzello, Antonia M. A., Ciardiello Acierno, Raffaele V., Carratore Verri, Tiziano G., DI PRISCO Storelli, Carlo Maffia, Michele 2007 STAMPA http://hdl.handle.net/11587/300517 https://doi.org/10.1007/s10930-007-9076-1 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000247473700006 volume:26(5) firstpage:335 lastpage:348 numberofpages:14 journal:PROTEIN JOURNAL http://hdl.handle.net/11587/300517 doi:10.1007/s10930-007-9076-1 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-34250816836 Gill carbonic anhydrase Antarctic fish haemoglobinless Chionodraco hamatu amino acid sequence S-glutathionylation info:eu-repo/semantics/article 2007 ftunivsalento https://doi.org/10.1007/s10930-007-9076-1 2024-03-28T01:40:50Z Gill cytoplasmic carbonic anhydrase of the haemoglobinless Antarctic icefish Chionodraco hamatus (Ice-CA) was directly sequenced and consists in 259 residues with an acetylated Nterminus. The molecular mass, deduced from the sequence, was 28.45 kDa, while mass spectrometry analysis of the native protein gave higher values. Treatment with dithiothreitol abolished this difference, indicating possible post-translational modifications. Isoelectric focusing analysis of Ice-CA suggested S-thiolation, which was identified as S-glutathionylation by immunostaining. Deglutathionylated Ice-CA maintained the anhydrase activity but showed higher susceptibility to hydrogen peroxide, suggesting that glutathione binding to Cys residues may have a role in the defence against oxidative damage. Ice-CA is characterized by lower thermal stability, higher activity and lower activation energy than its homologue gill CA of the temperate European eel, confirming the adaptation of the catalytic capacity to low temperatures. Alignment of Ice-CA with homologous enzymes from other fish shows high identity; the enzyme is grouped with a previously described fish CA monophyletic clade although Ice-CA shows several characteristics that can increase protein-solvent interaction and structural flexibility. Article in Journal/Newspaper Antarc* Antarctic Icefish Università del Salento: CINECA IRIS The Protein Journal 26 5 335 348 |
institution |
Open Polar |
collection |
Università del Salento: CINECA IRIS |
op_collection_id |
ftunivsalento |
language |
English |
topic |
Gill carbonic anhydrase Antarctic fish haemoglobinless Chionodraco hamatu amino acid sequence S-glutathionylation |
spellingShingle |
Gill carbonic anhydrase Antarctic fish haemoglobinless Chionodraco hamatu amino acid sequence S-glutathionylation RIZZELLO, Antonia ACIERNO, Raffaele VERRI, Tiziano STORELLI, Carlo MAFFIA, Michele M. A. CIARDIELLO V. CARRATORE G. DI PRISCO Biochemical characterization of a S-glutathionylated carbonic anhydrase isolated from gills of the Antarctic icefish Chionodraco hamatus |
topic_facet |
Gill carbonic anhydrase Antarctic fish haemoglobinless Chionodraco hamatu amino acid sequence S-glutathionylation |
description |
Gill cytoplasmic carbonic anhydrase of the haemoglobinless Antarctic icefish Chionodraco hamatus (Ice-CA) was directly sequenced and consists in 259 residues with an acetylated Nterminus. The molecular mass, deduced from the sequence, was 28.45 kDa, while mass spectrometry analysis of the native protein gave higher values. Treatment with dithiothreitol abolished this difference, indicating possible post-translational modifications. Isoelectric focusing analysis of Ice-CA suggested S-thiolation, which was identified as S-glutathionylation by immunostaining. Deglutathionylated Ice-CA maintained the anhydrase activity but showed higher susceptibility to hydrogen peroxide, suggesting that glutathione binding to Cys residues may have a role in the defence against oxidative damage. Ice-CA is characterized by lower thermal stability, higher activity and lower activation energy than its homologue gill CA of the temperate European eel, confirming the adaptation of the catalytic capacity to low temperatures. Alignment of Ice-CA with homologous enzymes from other fish shows high identity; the enzyme is grouped with a previously described fish CA monophyletic clade although Ice-CA shows several characteristics that can increase protein-solvent interaction and structural flexibility. |
author2 |
Rizzello, Antonia M. A., Ciardiello Acierno, Raffaele V., Carratore Verri, Tiziano G., DI PRISCO Storelli, Carlo Maffia, Michele |
format |
Article in Journal/Newspaper |
author |
RIZZELLO, Antonia ACIERNO, Raffaele VERRI, Tiziano STORELLI, Carlo MAFFIA, Michele M. A. CIARDIELLO V. CARRATORE G. DI PRISCO |
author_facet |
RIZZELLO, Antonia ACIERNO, Raffaele VERRI, Tiziano STORELLI, Carlo MAFFIA, Michele M. A. CIARDIELLO V. CARRATORE G. DI PRISCO |
author_sort |
RIZZELLO, Antonia |
title |
Biochemical characterization of a S-glutathionylated carbonic anhydrase isolated from gills of the Antarctic icefish Chionodraco hamatus |
title_short |
Biochemical characterization of a S-glutathionylated carbonic anhydrase isolated from gills of the Antarctic icefish Chionodraco hamatus |
title_full |
Biochemical characterization of a S-glutathionylated carbonic anhydrase isolated from gills of the Antarctic icefish Chionodraco hamatus |
title_fullStr |
Biochemical characterization of a S-glutathionylated carbonic anhydrase isolated from gills of the Antarctic icefish Chionodraco hamatus |
title_full_unstemmed |
Biochemical characterization of a S-glutathionylated carbonic anhydrase isolated from gills of the Antarctic icefish Chionodraco hamatus |
title_sort |
biochemical characterization of a s-glutathionylated carbonic anhydrase isolated from gills of the antarctic icefish chionodraco hamatus |
publishDate |
2007 |
url |
http://hdl.handle.net/11587/300517 https://doi.org/10.1007/s10930-007-9076-1 |
genre |
Antarc* Antarctic Icefish |
genre_facet |
Antarc* Antarctic Icefish |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000247473700006 volume:26(5) firstpage:335 lastpage:348 numberofpages:14 journal:PROTEIN JOURNAL http://hdl.handle.net/11587/300517 doi:10.1007/s10930-007-9076-1 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-34250816836 |
op_doi |
https://doi.org/10.1007/s10930-007-9076-1 |
container_title |
The Protein Journal |
container_volume |
26 |
container_issue |
5 |
container_start_page |
335 |
op_container_end_page |
348 |
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1796934080311328768 |