Back to Search
Start Over
The hemoglobin system of the brown moray Gymnothorax unicolor: structure/function relationships
The hemoglobin system of the brown moray Gymnothorax unicolor: structure/function relationships
- Source :
- 268 (2001): 4104–4111., info:cnr-pdr/source/autori:Tamburrini M.1, Verde C.1, Olianas A.2, Giardina B.3, Corda M.2, Sanna M.T.2, Fais A.2, Deiana A.M.2, di Prisco G.1, Pellegrini M.2/titolo:The hemoglobin system of the brown moray Gymnothorax unicolor. Structure%2Ffunction relationships./doi:/rivista:/anno:2001/pagina_da:4104/pagina_a:4111/intervallo_pagine:4104–4111/volume:268
- Publication Year :
- 2001
-
Abstract
- The Gymnothorax unicolor hemoglobin system is characterized by two components, called cathodic and anodic on the basis of their isoelectric point, which were separated by ion-exchange chromatography. The oxygen-binding properties of the purified components were studied in the absence and presence of chloride and/or GTP or ATP in the pH range 6.5-8.0. Stripped cathodic hemoglobin showed a small reverse Bohr effect, high oxygen affinity, and low co-operativity; the addition of chloride only caused a small decrease in oxygen affinity. In the presence of GTP or ATP, the oxygen affinity was dramatically reduced, the co-operativity increased, and the reverse Bohr effect abolished. Stripped anodic hemoglobin is characterized by both low oxygen affinity and co-operativity, and displayed a normal Bohr effect; the addition of chloride increased co-operativity, whereas ATP and GTP significantly modulated oxygen affinity at acidic pH values, enhancing the Bohr effect and giving rise to the Root effect. The complete amino-acid sequences of the alpha and beta chains of both hemoglobins were established; the molecular basis of the functional properties of the hemoglobins is discussed in the light of the primary structure and compared with those of other fish hemoglobins.
- Subjects :
- GTP'
Struttura
Molecular Sequence Data
Bohr effect
Biochemistry
Chloride
Effetto Bohr/Root
Phosphates
Hemoglobins
Gymnothorax unicolor
Allosteric Regulation
medicine
Animals
Amino Acid Sequence
Chromatography
Emoglobina
biology
Sequence Homology, Amino Acid
Chemistry
Root effect
Protein primary structure
Fishes
biology.organism_classification
Oxygen
Crystallography
Isoelectric point
Pesce
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Hemoglobin
Funzione
medicine.drug
Subjects
Details
- ISSN :
- 00142956
- Volume :
- 268
- Issue :
- 14
- Database :
- OpenAIRE
- Journal :
- European journal of biochemistry
- Accession number :
- edsair.doi.dedup.....26c57f513f99b0b452578e045b553970