Origin of the suppression of chloride ion sensitivity in human embryonic hemoglobin Gower II.
The molecular origin of the observed reduction of chloride ion sensitivity in the oxygen binding characteristics of the human embryonic hemoglobin Gower II has been probed by using site-directed mutant forms of the protein. Separate mutation of the three amino acids previously identified as candidates for the suppression of chloride sensitivity in the epsilon chain allowed us to unambiguously identify the His beta 77-->epsilon Asn as the origin of the lower sensitivity towards chloride ions in hemoglobin Gower II, which allows oxygen exchange from the mother to the late embryo under physiological conditions.
Zheng
T
T
School of Biological Sciences, University of Auckland, New Zealand.
Zhu
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Q
Brittain
T
T
D000328:Adult; D019943:Amino Acid Substitution / Q000235:genetics; D000838:Anions; D002712:Chlorides / Q000494:pharmacology*; D004622:Embryo, Mammalian; D006455:Hemoglobins, Abnormal / Q000235:genetics* / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D010100:Oxygen / Q000097:blood / Q000378:metabolism
D000838:Anions; D002712:Chlorides; D006455:Hemoglobins, Abnormal; C030446:hemoglobin Gower; D010100:Oxygen