Enhanced hemoglobin-oxygen unloading in migratory salmonids.

Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology (2017-12-09)
Jacelyn J Shu, Till S Harter, Phillip R Morrison, Colin J Brauner

Recent findings indicate that some teleost fishes may be able to greatly enhance hemoglobin-oxygen (Hb-O2) unloading at the tissues under conditions that result in catecholamine release. The putative mechanism relies on the high pH sensitivity of teleost hemoglobin (Hb), intracellular red blood cell (RBC) pH regulation via β-adrenergic Na+/H+ exchanger (β-NHE) activity, and plasma-accessible carbonic anhydrase at the tissues that short-circuits RBC pH regulation. Previous studies have shown that in rainbow trout, this system may double Hb-O2 unloading to red muscle compared to a situation without short-circuiting. The present study determined that: (1) in rainbow trout this system may be functional even at low concentrations of circulating catecholamines, as shown by conducting a dose-response analysis; (2) Atlantic and coho salmon also possess β-NHE activity, as shown by changes in hematocrit in adrenergically stimulated cells; and (3) with β-NHE short-circuiting, Atlantic and coho salmon may be able to increase Hb-O2 unloading by up to 74 and 159%, respectively, as determined by modeling based on O2 equilibrium curves. Together, these results indicate that a system to enhance Hb-O2 unloading may be common among salmonids and may be operational even under routine conditions. In view of the life histories of Atlantic and coho salmon, a system to enhance Hb-O2 unloading during exercise may help determine a successful spawning migration and thus reproductive success.

Product Number
Product Description

Heparin sodium salt from porcine intestinal mucosa, Grade I-A, ≥180 USP units/mg
Drabkin′s reagent, for the determination of hemoglobin
Carbonic Anhydrase from bovine erythrocytes, lyophilized powder, ≥2,000 W-A units/mg protein