title: Hemoglobin oxygen affinity is increased in erythropoietic protoporphyria.
abstract: Whole blood and hemolysates from seven normal and three erythropoietic protoporphyria patients were compared in terms of their hemoglobin function. The oxygen affinity (P50) of the erythropoietic protoporphyria hemolysates compared to normals (13.1 +/- 0.2 vs 17.5 +/- 0.3 mmHg; P < 0.001) and erythropoietic protoporphyria erythrocytes compared to normals (23.4 +/- 0.6 vs 27.1 +/- 0.5 mmHg; P < 0.001) were increased while oxygen-binding cooperativity (n-value of the Hill equation) were similar. We conclude that hemoglobin function in erythropoietic protoporphyria patients is altered, but without pathophysiologic consequences. Because hemoglobin in which protoporphyrin IX substitutes for heme has a low oxygen affinity, our findings of a higher than normal affinity in erythropoietic protoporphyria red cells and hemolysates may indirectly support the findings by others that protoporphyrin IX binds to hemoglobin at non-heme-binding sites. In addition, based on the effect of other abnormal hemoglobins, this shift in P50 will decrease any tendency for anemia in erythropoietic protoporphyria patients.
authors.affiliation: Department of Medicine, Albert Einstein College of Medicine, Bronx, NY.
authors.forename: R E
authors.initials: RE
authors.lastname: Hirsch
authors.forename: M J
authors.initials: MJ
authors.lastname: Lin
authors.forename: U R
authors.initials: UR
authors.lastname: Pulakhandam
authors.forename: R L
authors.initials: RL
authors.lastname: Nagel
authors.forename: S
authors.initials: S
authors.lastname: Sandberg
mesh_terms: D004912:Erythrocytes / Q000378:metabolism*; D005500:Follow-Up Studies; D006454:Hemoglobins / Q000378:metabolism*; D006461:Hemolysis; D006801:Humans; D007700:Kinetics; D010108:Oxyhemoglobins / Q000378:metabolism*; D017121:Porphyria, Hepatoerythropoietic / Q000097:blood*; D012016:Reference Values; D013997:Time Factors
chemical_list: D006454:Hemoglobins; D010108:Oxyhemoglobins