Résumé : After quantitative reaction of the sulfhydryl groups of chicken hemoglobins with para mercuribenzoate, α and β chains cannot be separated by chromatography from either major or minor component. Ultracentrifugations show that dissociation into dimers occurs, but at protein concentrations much lower than those observed for mammalian hemoglobins. Oxygen equilibrium is affected: cooperative effects are weakened and oxygen affinity increases, the amplitude of the alteration being different for each component in presence or in absence of inositol hexaphosphate. Comparison with the behaviour of some mammalian hemoglobins is discussed. © 1973.