Genetic diversity of coastal bottlenose dolphins revealed by structurally and functionally diverse hemoglobins.
Genetic diversity of coastal bottlenose dolphins revealed by structurally and functionally diverse hemoglobins.
复制标题
结构和功能多样化的血红蛋白揭示了沿海宽吻海豚的遗传多样性。
DOI:
10.1016/j.gene.2007.02.050
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发表时间:
2007
期刊:
影响因子:
3.5
通讯作者:
Bonaventura,Celia
中科院分区:
文献类型:
--
作者:
Remington,Nicole;Stevens,RobertD;Wells,RandallS;Holn,Aleta;Dhungana,Suraj;Taboy,CelineH;Crumbliss,AlvinL;Henkens,Robert;Bonaventura,Celia
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 enhances 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.