Very rare. Abnormal hemoglobin due to a mutation in position 102 on the α chain where aspartic acid is replaced by tyrosine. Even in the heterozygous state, this mutation causes a decrease in the affinity of hemoglobin for O2 with a right shift of the hemoglobin dissociation curve. This deviation decreases once the pH is alkalinized.

Anesthetic implications: 

falsely low pulse oximetry values in room air.

References : 

-         Poyart C, Schaad O, Kister J, Galacteros F et al. 
Hemoglobin Saint Mandé : functional studies and structural modeling reveal an altered T state. 
Eur J Biochem 1990 ; 194 : 343-8

-        Eguienta S, Martigne L, Dulucq S, Fayon M. 
Pièges de la mesure de la saturation de l’hémoglobine en oxygène : à propos d’un cas de désaturation chronique. 
Arch Pédiatr 2015 ; 22 : 390-2.

Updated: March 2019