Abstract
From being the first protein to have its three‐dimensional structure determined to being sequenced for hundreds of species, myoglobin (Mb) has had a distinguished history as a research subject. Although Mb is one of the most studied proteins, surprisingly little is known of its oxygen affinity at physiologically significant temperature or the variability of this oxygen affinity between species. In this study we compared the oxygen affinity (P50) of skeletal muscle Mb from six terrestrial and ten diving vertebrates. After extracting Mb from muscle samples and removing hemoglobin contamination, oxygen affinity was determined using a TCS Hemox Blood Analyzer. We found Mb P50 ranging from 2.5 to 5.3 mmHg at 37°C. Modeling of oxygen transport in muscle tissue will be necessary to determine if this twofold difference in oxygen affinity has significant implications in oxygen transport under various physiological conditions. Variants in Mb structure and function could be adaptive for species that regularly experience muscle hypoxia such as diving vertebrates.
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