The primary structure of hemoglobin from reindeer (Rangifer tarandus tarandus) and its functional implications

The primary structures of alpha- and beta-chains of hemoglobin from reindeer (Rangifer tarandus tarandus) were determined. Comparison of the reindeer hemoglobin sequence with those of human and bovine hemoglobins showed 50 and 29 substitutions per alpha beta dimer, respectively. The influence of rep...

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Bibliographic Details
Main Authors: Petruzzelli, R, Barra, D, Bossa, F, Brix, O, Nuutinen, M, Giardina, B., CONDO', SAVERIO GIOVANNI
Other Authors: Condo', Sg, Giardina, B
Format: Article in Journal/Newspaper
Language:English
Published: 1991
Subjects:
Animal
Cattle
Oxyhemoglobin
Hemoglobin
Sequence Homology
Nucleic Acid
Human
Molecular Sequence Data
Amino Acid Sequence
Reindeer
Deer
Settore BIO/10 - BIOCHIMICA
Rangifer tarandus
Online Access:http://hdl.handle.net/2108/54790
Description
Summary:The primary structures of alpha- and beta-chains of hemoglobin from reindeer (Rangifer tarandus tarandus) were determined. Comparison of the reindeer hemoglobin sequence with those of human and bovine hemoglobins showed 50 and 29 substitutions per alpha beta dimer, respectively. The influence of replacements on the modulation of hemoglobin oxygen affinity by heterothopic ligands and temperature, as well as their importance on the structure-function relationships in hemoglobin are discussed.

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