Characteristics of the anion transport system in sea turtle erythrocytes.

Erythrocytes of Kemp's ridley sea turtle (Lepidochelys kempi) contain a 100- to 105-kDa protein that is reactive with a monoclonal antibody to the membrane domain of human erythrocyte band 3. Based on inhibition of membrane HCO(3-)-Cl- exchange with 4-acetamido-4'-isothiocyanostilbene-2,2'-disulfonic acid (SITS), sea turtle erythrocytes were found to contain 4 x 10(6) copies of band 3 per cell. Unidirectional HCO3- transfer, specifically HCO3- out----in-Cl-in----out exchange, where subscript in----out represents transfer from inside to outside and subscript out----in represents transfer from outside to inside, was characterized by a maximal exchange rate of 1.0-1.1 nmol.cm-2.s-1, substrate affinity coefficients of 0.1-0.2 mM for HCO3- and 1.6 mM for Cl-, and an apparent inhibition constant for SITS of 0.6-1.0 microM (10 degrees C, pH 7.6). Under physiological conditions (30 degrees C, pH 7.4), the rate of net HCO3- transfer (i.e., the difference between HCO3- in----out-Cl-out----in and HCO3- out----in-Cl-in----out) was 1.13 nmol. cm-2.s-1 for cells subjected to a 5-mM decrement in CO2 content. This yields a rate coefficient for the "physiological" anion shift in sea turtle blood of 1.7 s-1, indicating that the anion shift may require 2.6 s to reach 99% completion in vivo. The erythrocyte anion shift appears to be a potential rate-limiting step for capillary CO2 exchange in these turtles.