Myoglobin Adaptation in Terrestrial and Diving Birds and Mammals

Myoglobin (Mb) is an oxygen binding hemoprotein in vertebrate skeletal muscle that functions in intracellular oxygen storage and transport. Due to the unique oxygen storage demands of diving birds and mammals, these vertebrates can have Mb concentrations ten-fold those found in their terrestrial cou...

Full description

Bibliographic Details
Main Author: Wright, Traver J.
Other Authors: Davis, Randall, Marshall, Christopher, Neill, William, Wasser, Jeremy
Format: Thesis
Language:English
Published: 2015
Subjects:
Online Access:https://hdl.handle.net/1969.1/152831
id fttexasamuniv:oai:oaktrust.library.tamu.edu:1969.1/152831
record_format openpolar
spelling fttexasamuniv:oai:oaktrust.library.tamu.edu:1969.1/152831 2023-07-16T04:01:14+02:00 Myoglobin Adaptation in Terrestrial and Diving Birds and Mammals Wright, Traver J. Davis, Randall Marshall, Christopher Neill, William Wasser, Jeremy 2015-01-09T20:52:21Z application/pdf https://hdl.handle.net/1969.1/152831 en eng https://hdl.handle.net/1969.1/152831 myoglobin oxygen affinity marine mammal diving adaptation evolution Thesis text 2015 fttexasamuniv 2023-06-27T22:56:39Z Myoglobin (Mb) is an oxygen binding hemoprotein in vertebrate skeletal muscle that functions in intracellular oxygen storage and transport. Due to the unique oxygen storage demands of diving birds and mammals, these vertebrates can have Mb concentrations ten-fold those found in their terrestrial counterparts making them ideal animal models for studying Mb function. Increased Mb bound muscle oxygen stores are advantageous for diving vertebrates, but Mb concentration optimized to maintain aerobic metabolism while diving or limiting to aerobic dive duration? A numeric model simulating a diving Weddell seal was created to examine physiological factors that influence dive duration and optimal Mb concentration. Mb concentration was limiting to dive duration in postabsorptive dives. However, Mb concentration was optimized for postprandial dives which were limited by blood-bound oxygen stores due to the additional metabolic costs of digestion. While Mb concentration is adaptive in diving vertebrates, less is known about molecular adaptation of Mb functional properties. Novel methods were developed to extract Mb from frozen muscle and determine Mb oxygen affinity (P_(50)) by generating a high resolution oxygen dissociation curve at 37°C. For comparison, Mb P_(50) was determined for 25 species of diving and terrestrial birds and mammals. Myoglobin P_(50) was conserved among terrestrial vertebrates and most cetaceans at approximately 3.7 mmHg with the exception of the melon-headed whale that had a significantly higher P_(50) (lower oxygen affinity) of 4.85 mmHg. Among pinnipeds (seals and sea lions) the P_(50) ranged from 3.23-3.81 mmHg and showed a trend for higher oxygen affinity in species with longer dive durations. Among diving birds the P_(50) ranged from 2.40-3.36 mmHg and also showed a trend of higher affinities in species with longer dive durations. Both myoglobin concentration and oxygen affinity appear adaptive in diving vertebrates to maintain aerobic metabolism and minimize hypoxic cellular damage in ischemic ... Thesis Weddell Seal Texas A&M University Digital Repository Weddell
institution Open Polar
collection Texas A&M University Digital Repository
op_collection_id fttexasamuniv
language English
topic myoglobin
oxygen affinity
marine mammal
diving
adaptation
evolution
spellingShingle myoglobin
oxygen affinity
marine mammal
diving
adaptation
evolution
Wright, Traver J.
Myoglobin Adaptation in Terrestrial and Diving Birds and Mammals
topic_facet myoglobin
oxygen affinity
marine mammal
diving
adaptation
evolution
description Myoglobin (Mb) is an oxygen binding hemoprotein in vertebrate skeletal muscle that functions in intracellular oxygen storage and transport. Due to the unique oxygen storage demands of diving birds and mammals, these vertebrates can have Mb concentrations ten-fold those found in their terrestrial counterparts making them ideal animal models for studying Mb function. Increased Mb bound muscle oxygen stores are advantageous for diving vertebrates, but Mb concentration optimized to maintain aerobic metabolism while diving or limiting to aerobic dive duration? A numeric model simulating a diving Weddell seal was created to examine physiological factors that influence dive duration and optimal Mb concentration. Mb concentration was limiting to dive duration in postabsorptive dives. However, Mb concentration was optimized for postprandial dives which were limited by blood-bound oxygen stores due to the additional metabolic costs of digestion. While Mb concentration is adaptive in diving vertebrates, less is known about molecular adaptation of Mb functional properties. Novel methods were developed to extract Mb from frozen muscle and determine Mb oxygen affinity (P_(50)) by generating a high resolution oxygen dissociation curve at 37°C. For comparison, Mb P_(50) was determined for 25 species of diving and terrestrial birds and mammals. Myoglobin P_(50) was conserved among terrestrial vertebrates and most cetaceans at approximately 3.7 mmHg with the exception of the melon-headed whale that had a significantly higher P_(50) (lower oxygen affinity) of 4.85 mmHg. Among pinnipeds (seals and sea lions) the P_(50) ranged from 3.23-3.81 mmHg and showed a trend for higher oxygen affinity in species with longer dive durations. Among diving birds the P_(50) ranged from 2.40-3.36 mmHg and also showed a trend of higher affinities in species with longer dive durations. Both myoglobin concentration and oxygen affinity appear adaptive in diving vertebrates to maintain aerobic metabolism and minimize hypoxic cellular damage in ischemic ...
author2 Davis, Randall
Marshall, Christopher
Neill, William
Wasser, Jeremy
format Thesis
author Wright, Traver J.
author_facet Wright, Traver J.
author_sort Wright, Traver J.
title Myoglobin Adaptation in Terrestrial and Diving Birds and Mammals
title_short Myoglobin Adaptation in Terrestrial and Diving Birds and Mammals
title_full Myoglobin Adaptation in Terrestrial and Diving Birds and Mammals
title_fullStr Myoglobin Adaptation in Terrestrial and Diving Birds and Mammals
title_full_unstemmed Myoglobin Adaptation in Terrestrial and Diving Birds and Mammals
title_sort myoglobin adaptation in terrestrial and diving birds and mammals
publishDate 2015
url https://hdl.handle.net/1969.1/152831
geographic Weddell
geographic_facet Weddell
genre Weddell Seal
genre_facet Weddell Seal
op_relation https://hdl.handle.net/1969.1/152831
_version_ 1771550876088926208