PROPERTIES OF TROUT HBI IN WATER AND LIGAND LINKED BINDING OF NA+

Bruno Giardina, L Airoldi, M Brunori

Risultato della ricerca: Contributo in rivistaArticolo in rivista

5 Citazioni (Scopus)

Abstract

The structural and functional properties of trout Hb I (one of the components isolated from the hemo- lysate of trout, Salmo irideus) have been investigated in considerable detail in the last few years [l-l]. Its properties are exceptional in sofar as ligand binding is characterized by strong heme-heme interactions but lacks completely effects of protons and organic phos- phates. We have investigated the functional properties of trout Hb I in water and in various salts. From the experiments in pure water it is clear that the equilib- rium and kinetics of the isoionic protein are very sim- ilar to those obtained in buffered solutions at different pH values [l-4]. This leads to the conclusion that the characteristic thermodynamic properties of trout Hb I [3] are intrinsic features of the system, and are not dominated by heterotropic effects involving small ions. In addition the oxygen equilibrium of trout Hb I investigated as a function of NaCl, sodium citrate and sodium dextran sulfate shows two distinct effects, one related to the differential binding of Cl- [5] and the other to the specific binding of Na+, which is proven to stabilize the low affinity conformational state of hemoglobin. This effect is discussed in the light of the known structural properties of trout Hb I.
Lingua originaleEnglish
pagine (da-a)273-276
Numero di pagine4
RivistaFEBS Letters
Volume129
DOI
Stato di pubblicazionePubblicato - 1981

Keywords

  • FISH HEMOGLOBINS
  • Na+ bindings

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