Isolation and characterization of a carbonic anhydrase homologue from the zebrafish (Danio rerio).
We have isolated a 29,000-Da carbonic anhydrase (CA) protein from the zebrafish, Danio rerio, sequenced two peptide fragments, and tentatively identified it as a high-activity CA by inhibition kinetics. We have also characterized a 1,537-bp message whose deduced sequence of 260 amino acids matches that of the isolated protein. This CA is clearly an alpha-CA based on the similarity of its sequence to that of other members of the alpha-CA gene family. A phylogenetic analysis suggested CAH-Z diverged after the branching of the CA-V and CA-VII genes and prior to the duplications that generated the CA-I, CA-II, and CA-III genes of amniotes. This marks the first characterization of the mRNA and its protein product from the CA gene of a teleost.
Peterson
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The Whitney Laboratory, University of Florida, 9505 Ocean Shore Blvd., St. Augustine, FL 32086-8623, USA. REP@whitney.ufl.edu
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Linser
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002256:Carbonic Anhydrases / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D003001:Cloning, Molecular; D017931:DNA Primers; D019143:Evolution, Molecular; D014644:Genetic Variation; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D010802:Phylogeny; D015027:Zebrafish / Q000235:genetics*
D017931:DNA Primers; D007527:Isoenzymes; D002256:Carbonic Anhydrases