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Molecular structure and functional adaptations of hemoglobins from Antarctic marine organisms

 

作者: Guido di Prisco,   Vito Carratore,   Ennio Cocca,   Antonio Riccio,   Maurizio Tamburrini,  

 

期刊: Italian Journal of Zoology  (Taylor Available online 2000)
卷期: Volume 67, issue sup1  

页码: 37-46

 

ISSN:1125-0003

 

年代: 2000

 

DOI:10.1080/11250000009356354

 

出版商: Taylor & Francis Group

 

关键词: Hemoglobin;Myoglobin;Protein structure;Oxygen binding;Gene organisation;Adaptive evolution

 

数据来源: Taylor

 

摘要:

This research dealing with fish, bird and mammal hemoglobins is in the framework of the study of the molecular basis of cold adaptation in Antarctic organisms. The study of hemoglobin structural and functional properties in Antarctic teleosts allowed a correlation of amino acid sequence, multiplicity, and oxygen‐binding features with ecological constraints. Amino acid sequences of α and β chains were analysed to build phylogenetic trees, while the organisation and expression of globin genes was studied. The respiratory proteins of Antarctic birds were investigated, in relation with the oxygen demands arising from their characteristic behaviour (diving or flight) and, in general, from the extreme conditions of the Antarctic habitat. The study of Weddell seal hemoglobins indicated that the combined effect of carbon dioxide, organic phosphates and temperature optimises oxygen delivery to all tissues in spite of their relative heterothermia. The crystallographic structure of the carbonmonoxy derivative ofTrematomus newnesimajor hemoglobin was resolved, giving new insight into the study of the Root effect. The molecular models of skua hemoglobins revealed the presence of a second, additional phosphate binding site located between the two α chains, paving the way to further studies.

 

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