Studies of structure-function relationships in the respiratory proteins of marine mammals revealed unexpected variations in the number and types of hemoglobins (Hbs) present in coastal bottlenose dolphins, Tursiops truncatus. We obtained blood samples from free-ranging coastal bottlenose dolphins as a component of capture-release studies. We found that the oxygen-binding functions of bottlenose dolphin blood are poised between effector-saturated and unsaturated levels, enabling exercise-dependent shifts in oxygen transfer functions. Isolated bottlenose dolphin Hbs showed elevated pH sensitivities (Bohr effects) and appreciably lower oxygen affinities than adult human Hb in the absence of allosteric effectors. These properties may be an adaptive modification that enhance oxygen delivery during diving episodes when oxygen tensions and effector levels are low. The Hbs of individual dolphins showed similar oxygen affinities, responses to effectors, and expression of heme-heme interaction in oxygen binding, but differed in their redox potentials and rates of autoxidation. The heterogeneity suggested by these functional variations in Hbs of individual dolphins was born out by variations in the molecular weights and numbers of their α and β globin chains. Although coastal bottlenose dolphins were expected to have a single type of Hb, the mass differences observed revealed considerable genetic diversity. There were multiple Hb forms in some individuals and differences in Hb patterns among individuals within the same community.Keywords population diverstiy; alleles; oxygen binding; allostery; redox chemistry *Address correspondence to: Celia Bonaventura, Duke University Marine Laboratory, Beaufort, NC 28516, Tel. 252−505−7591; Fax 252−728−6824, E-Mail: bona@duke.edu.. Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.
IntroductionBottlenose dolphins are widely distributed in both coastal and offshore waters throughout the world. Their relatively easy accessibility by researchers has made them one of the most frequently studied marine mammals (Leatherwood and Reeves, 1990). Despite this, few studies have sought to describe the characteristics of bottlenose dolphin hemoglobin (Hb). Our studies add to knowledge of these diving mammals by documenting exercise-dependent oxygenbinding functions of whole blood, by determining oxygen binding and oxidative functions of bottlenose dolphin Hb in the presence and absence of allosteric effectors, and by showing an unexpected diversity in coastal bottlenose dolphins Hbs.Hb is found in the erythrocytes of dolphins and other vertebrates and...