Haemoglobin Hammersmith (β 42 (CD1) Phe→Ser)

Altered sulfhydryl reactivity of hemoglobins and red blood cell membranes in congenital heinz body hemolytic anemia

“…The abnormal hemoglobin, which constituted approximately 20%o of the total hemoglobin content of hemolysates, was identified by column and paper chromatographic purification, and peptide fingerprinting techniques performed and described by Carrell, Lehmann, and Hutchison (13). In addition, blood from one other splenectomized patient with a more severe anemia whose Heinz body red cells contained another unstable hemoglobin, Hammersmithl PU phenylalanine .> serine (14), was used in some studies. Observations on this patient's blood suggest that the mechanisms of Heinz body formation, hemolytic anemia, and dipyrroluria proposed for hemoglobin Koln have relevance for other unstable hemoglobins as well.…”

An erythroid chaperone that facilitates folding of α-globin subunits for hemoglobin synthesis

“…Apo-α-globin is extremely unstable in solution and in cells. In vitro studies and analysis of globin mutations in patients demonstrate that heme insertion stabilizes the native structure of apo-globins (37,(46)(47)(48). Previous studies demonstrated that AHSP binds apo-α-globin (32).…”

Hemoglobin Okaloosa (β48 (CD7) Leucine → Arginine). AN UNSTABLE VARIANT WITH LOW OXYGEN AFFINITY

“…Buffer composition (19) and ionic strength fiT-6 fT-7 fiT-8 fT-9 fT-10 fiT-11 fT-12A fiT-12B fT-13 fiT-14 fT-15 It is not apparent why substitution of arginine for leucine at position CD7 produces decreased oxygen affinity and increased heat precipitability, but similar abnormalities have been observed in hemoglobins produced by neighboring mutations. Four unstable hemoglobins with decreased oxygen affinity are produced by substitutions at position CD1 (Hammersmith [21], Louisville [3], Bucuresti [22], and Torino [23]). These hemoglobins are quite unstable, and carriers have clinically significant hemolytic anemia.…”