Article

The amino acid sequence of the single hemoglobin of the high-antarctic fish Bathydraco marri Norman.

Institute of Protein Biochemistry and Enzymology, Consiglio Nazionale delle Ricerche, Naples, Italy.
Comparative biochemistry and physiology. B, Comparative biochemistry 09/1992; 102(4):941-6. pp.941-6
Source: PubMed

ABSTRACT 1. Bathydraco marri Norman is a cold-adapted Antarctic teleost (Family: Bathydraconidae), living preferably at depths between 400 and 1200 m. 2. The blood of this species contains a single hemoglobin, in which oxygen binding is pH-regulated (Bohr and Root effects). 3. The complete amino acid sequence of the alpha and beta chains of the hemoglobin of B. marri has been elucidated.

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Keywords

beta chains
 
Bohr
 
cold-adapted Antarctic teleost
 
complete amino acid sequence
 
oxygen binding
 
Root effects
 
single hemoglobin