ArticleJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology2004
Comparative physiology and molecular analysis of carbonic anhydrase from the red blood cells of teleost fish.
Article in Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 40 citations in OpenAlex.
- The importance of a single amino acid substitution in reduced red blood cell carbonic anhydrase function of early-diverging fish.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2020Article
- A cytosolic carbonic anhydrase molecular switch occurs in the gills of metamorphic sea lamprey.Scientific reports · 2016Article
- Gymnocypris przewalskii decreases cytosolic carbonic anhydrase expression to compensate for respiratory alkalosis and osmoregulation in the saline-alkaline lake Qinghai.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2016Article
- Phosphorylation increases the catalytic activity of rainbow trout gill cytosolic carbonic anhydrase.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2016Article
- Biochemical characterization of a S-glutathionylated carbonic anhydrase isolated from gills of the Antarctic icefish Chionodraco hamatus.The protein journal · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This study investigates the early evolution of vertebrate red blood cell (rbc) carbonic anhydrase (CA) by examining the physiological and molecular properties of rbc CA in teleost fish. When representatives of four different families of teleosts were compared, it was found that differences in overall rbc CA activity were due to different concentrations of CA, rather than differences in the enzyme's kinetic properties. Additional molecular analysis of CA from the rbcs of rainbow trout provided further evidence that critical elements of the enzyme, such as the active site, have been highly conserved during vertebrate evolution. The active site of the trout CA differed from that of gar rbc CA at only two amino acid positions. The rainbow trout rbc CA sequence also showed high sequence homology with CA sequences from other fish tissues, and fits into an emerging group of fish CAs that are basal to mammalian CA I, II and III. Northern blot analysis of the tissue expression of the sequenced CA indicated that it is primarily found in the rbcs, but high amounts of cytosolic CA activity were also found in the gill, suggesting the presence of other cytosolic CA isozymes in this species.
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