Hemoglobin Ypsilanti: A High-Oxygen-Affinity Hemoglobin
Hemoglobin Ypsilanti: A High-Oxygen-Affinity Hemoglobin
Hemoglobin (Hb) Ypsilanti is a rare high-oxygenaffinity hemoglobin. Like other high-oxygen-affinity hemoglobins, Hb Ypsilanti manifests as erythrocytosis. Because the migration of many high-oxygen-affinity variants on alkaline and acid gels does not differ from that of HbA, oxygen-hemoglobin dissociation studies are often used to document their presence. Hb Ypsilanti is a notable exception because its electrophoresis pattern on alkaline gel is highly characteristic, exemplifying the phenomenon of hybrid formation in variant hemoglobins. In the past few years, several laboratories have begun to use high-pressure liquid chromatography (HPLC) as a screen for hemoglobinopathies. We demonstrate the elution profile of Hb Ypsilanti on the 2 most widely used HPLC methods.
Hemoglobin (Hb) Ypsilanti is a rare, high-oxygen-affinity hemoglobin first described in 1967 and named for the Michigan city in which the index family resided. Like other high-oxygen-affinity hemoglobins, of which there are now substantially more than 100 described, Hb Ypsilanti manifests as erythrocytosis. Because the migration of many high-oxygen- affinity variants on alkaline and acid gels does not differ from that of HbA, oxygen-hemoglobin dissociation studies are often used to document their presence. Hb Ypsilanti is a notable exception because its electrophoresis pattern on alkaline gel is highly characteristic, representing the formation of hybrids of the variant hemoglobin.
In the past few years, several laboratories have begun to use high-pressure liquid chromatography (HPLC) as a screen for hemoglobinopathies. This report describes the elution profile of Hb Ypsilanti on the 2 most widely used HPLC methods.
Abstract and Introduction
Abstract
Hemoglobin (Hb) Ypsilanti is a rare high-oxygenaffinity hemoglobin. Like other high-oxygen-affinity hemoglobins, Hb Ypsilanti manifests as erythrocytosis. Because the migration of many high-oxygen-affinity variants on alkaline and acid gels does not differ from that of HbA, oxygen-hemoglobin dissociation studies are often used to document their presence. Hb Ypsilanti is a notable exception because its electrophoresis pattern on alkaline gel is highly characteristic, exemplifying the phenomenon of hybrid formation in variant hemoglobins. In the past few years, several laboratories have begun to use high-pressure liquid chromatography (HPLC) as a screen for hemoglobinopathies. We demonstrate the elution profile of Hb Ypsilanti on the 2 most widely used HPLC methods.
Introduction
Hemoglobin (Hb) Ypsilanti is a rare, high-oxygen-affinity hemoglobin first described in 1967 and named for the Michigan city in which the index family resided. Like other high-oxygen-affinity hemoglobins, of which there are now substantially more than 100 described, Hb Ypsilanti manifests as erythrocytosis. Because the migration of many high-oxygen- affinity variants on alkaline and acid gels does not differ from that of HbA, oxygen-hemoglobin dissociation studies are often used to document their presence. Hb Ypsilanti is a notable exception because its electrophoresis pattern on alkaline gel is highly characteristic, representing the formation of hybrids of the variant hemoglobin.
In the past few years, several laboratories have begun to use high-pressure liquid chromatography (HPLC) as a screen for hemoglobinopathies. This report describes the elution profile of Hb Ypsilanti on the 2 most widely used HPLC methods.