|Titolo:||The hemoglobin system of the brown moray Gymnothorax unicolor: structure/function relationships|
|Data di pubblicazione:||2001|
|Citazione:||The hemoglobin system of the brown moray Gymnothorax unicolor: structure/function relationships / Tamburrini M; Verde C; Olianas A; Giardina B; Corda M; Sanna M T; Fais A; Deiana A M; Di Prisco G; Pellegrini M. - In: EUROPEAN JOURNAL OF BIOCHEMISTRY. - ISSN 0014-2956. - 268:14(2001), pp. 4104-4111.|
|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 effects 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.|
|Tipologia:||1.1 Articolo in rivista|
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