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First published online March 17, 2006
Journal of Experimental Biology 209, 1169-1178 (2006)
Published by The Company of Biologists 2006
doi: 10.1242/jeb.02111
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Tribute to R. G. Boutilier: Evidence of a high activity carbonic anhydrase isozyme in the red blood cells of an ancient vertebrate, the sea lamprey Petromyzon marinus

A. J. Esbaugh* and B. L. Tufts

Department of Biology, Queen's University, Kingston, Ontario, K7L 3N6, Canada


Figure 1
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  		Fig. 1. Nucleotide and deduced amino acid sequence of lamprey rbc carbonic anhydrase. The sequence shown is the coding region only, from start codon (underlined) to stop codon (asterisk), as determined through RACE (rapid amplification of cDNA ends).

 

Figure 2
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  		Fig. 2. Representative northern blots for lamprey cytoplasmic carbonic anhydrase (CA) and haemoglobin (Hb) mRNA, and 18S rRNA from perfused adult lamprey tissues (N=4). RBC, red blood cell.

 

Figure 3
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  		Fig. 3. Carbonic anhydrase (CA) activity in the cytosolic fraction of perfused adult lamprey tissues. Values are means ± s.e.m. (N=4), with statistically different groups indicated by different letters (P<0.05). RBC, red blood cell.

 

Figure 4
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  		Fig. 4. Phylogenetic analysis of cytoplasmic lamprey carbonic anhydrase and other cytoplasmic {alpha}-carbonic anhydrase isozymes. The phylogenetic tree was constructed using neighbour joining analysis with support for nodes assessed using bootstrap analysis. The tree was ordered using human carbonic anhydrase Va and Vb as a monophyletic outgroup. Branches are drawn to scale (bar) with the length of 0.1 approximating replacement of 10% of the amino acids in the protein alignment (no Poisson correction for multiple hits).

 




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