Journal of Comparative Physiology B

, Volume 163, Issue 5, pp 380–388 | Cite as

The distribution of carbonic anhydrase type I and II isozymes in lamprey and trout: possible co-evolution with erythrocyte chloride/bicarbonate exchange

  • Raymond P. Henry
  • Bruce L. Tufts
  • Robert G. Boutilier
Article

Abstract

The subcellular distribution and kinetic properties of carbonic anhydrase were examined in red blood cells and gills of the lamprey, Petromyzon marinus, a primitive agnathan, and rainbow trout, Oncorhynchus mykiss, a modern teleost, in relation to the evolution of rapid Cl/HCO 3 exchange in the membrane of red blood cells. In the lamprey, which either lacks or has minimal red cell Cl/HCO 3 exchange, there has been no compensatory incorporation of carbonic anhydrase into the membrane fraction of either the red cell or the gill. Carbonic anhydrase activity in red cells is exclusively cytoplasmic, and the single isozyme displays kinetic properties typical of the type I, slow turnover, isozyme. In the red blood cells of the trout, however, which possess high amounts of the band-3 Cl/HCO 3 exchange protein, the single carbonic anhydrase isozyme appears to be kinetically similar to the type II, fast turnover, isozyme. It thus appears that the type I isozyme present in the red blood cells of primitive aquatic vertebrates was replaced in modern teleosts by the kinetically more efficient type II isozyme only after the incorporation and expression of a significant amount of the band-3 exchange protein in the membrane of the red cell.

Key words

Carbonic anhydrase Cl/HCO3 exchange Red blood cells Lamprey, Petromyzon Trout, Oncorhynchus 

Abbreviations

BCIP

5-bromo-4-chloro-3-indolyl phosphate

CA

carbonic anhydrase

DTT

dithiothreitol

EDTA

ethylenediaminetetra-acetate

E0

total concentration of free enzyme

i

fractional inhibition of enzyme activity

IU

international units

K1

inhibition constant

KM

Michaelis constant

NBT

nitro blue tetrazolium

NCP

nitrocellulose paper

RBC

red blood cell

SDS-PAGE

sodium dodecyl sulphate polyacrylamide gel electrophoresis

Vmax

maximal velocity of reaction

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Copyright information

© Springer-Verlag 1993

Authors and Affiliations

  • Raymond P. Henry
    • 1
    • 2
  • Bruce L. Tufts
    • 3
  • Robert G. Boutilier
    • 4
  1. 1.Department of ZoologyAuburn UniversityAuburnUSA
  2. 2.the Alabama Agricultural Experiment StationAuburn UniversityAuburnUSA
  3. 3.Department of BiologyQueens UniversityKingstonCanada
  4. 4.Department of ZoologyUniversity of CambridgeCambridgeUK

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