-transparent.png){kind=logo}
Hb Iowa with a Gly----Ala mutation at position beta 119(GH2) was observed in a Black infant and her mother. The baby was also heterozygous for Hb S; Hb Iowa was confused with Hb F at birth because its electrophoretic mobility was similar to that of Hb F1. The beta chain of Hb Iowa could be readily separated from the beta A, alpha, and gamma chains by polyacrylamide gel electrophoresis and by reversed phase high performance liquid chromatography. Structural characterization was through amino acid analyses of peptides isolated from a tryptic digest of the aminoethylated beta-Iowa chain. The Gly----Ala replacement in Hb Iowa does not affect its stability and oxygen carrying properties; hematological data for mother and child were within normal ranges.
D Plaseska, and
P A de Alarcon, and
S McMillan, and
M Walbrecht, and
J B Wilson, and
T H Huisman
January 1981,
Hemoglobin,
D Plaseska, and
P A de Alarcon, and
S McMillan, and
M Walbrecht, and
J B Wilson, and
T H Huisman
December 1976,
Biochimica et biophysica acta,
D Plaseska, and
P A de Alarcon, and
S McMillan, and
M Walbrecht, and
J B Wilson, and
T H Huisman
January 1989,
Hemoglobin,
D Plaseska, and
P A de Alarcon, and
S McMillan, and
M Walbrecht, and
J B Wilson, and
T H Huisman
January 1985,
Hemoglobin,
D Plaseska, and
P A de Alarcon, and
S McMillan, and
M Walbrecht, and
J B Wilson, and
T H Huisman
January 1981,
Sangre,
D Plaseska, and
P A de Alarcon, and
S McMillan, and
M Walbrecht, and
J B Wilson, and
T H Huisman
January 1979,
Hemoglobin,
D Plaseska, and
P A de Alarcon, and
S McMillan, and
M Walbrecht, and
J B Wilson, and
T H Huisman
January 1989,
Hemoglobin,
D Plaseska, and
P A de Alarcon, and
S McMillan, and
M Walbrecht, and
J B Wilson, and
T H Huisman
August 1994,
Annals of hematology,
D Plaseska, and
P A de Alarcon, and
S McMillan, and
M Walbrecht, and
J B Wilson, and
T H Huisman
January 1985,
Hemoglobin,
D Plaseska, and
P A de Alarcon, and
S McMillan, and
M Walbrecht, and
J B Wilson, and
T H Huisman
January 1989,
Hemoglobin,
