Hb Okazaki [β93(F8) Cys → Arg], a new hemoglobin variant with increased oxygen affinity and instability
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Summary
A new abnormal hemoglobin, Hb Okazaki, with an amino acid substitution at the tyrosine pocket of the β chain as well as at the α2β1 contact of the quaternary structure of molecule, was discovered in a Japanese man.
- Type
- article
- Published
- 1984-07-23
- Cited by
- 25
- References
- 8
- Access
- Open access
- OpenAlex
- https://openalex.org/W1997370544
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:38615825
Keywords
Okazaki fragments, Hemoglobin, Chemistry, BETA (programming language), Oxygen
References
- Estimation of Small Percentages of Fœtal Hæmoglobin
- Measurement of accurate oxygen equilibrium curves by an automatic oxygenation apparatus.
- Identification of Residues responsible for the Alkaline Bohr Effect in Haemoglobin
- A Textbook of Clinical Pathology
- A Simple Method for the Detection of Unstable Haemoglobins
- Rapid differentiation of polypeptide chains of hemoglobin by cellulose acetate electrophoresis of hemolylsates.
Cited by
- Low concentrations of nitric oxide increase oxygen affinity of sickle erythrocytes in vitro and in vivo.
- Reply to “SNO-hemoglobin and hypoxic vasodilation”
- Hb Riesa or β93 (F9) Cys→Ser, a new electrophoretically silent haemoglobin variant interfering with haemoglobin A1c measurement.
- Unexpectedly low pulse oximetry measurements associated with variant hemoglobins: A systematic review
- Biochemical Characterization of HumanS-Nitrosohemoglobin
- Biochemical characterization of S-nitrosohemoglobin. Mechanisms underlying synthesis, no release, and biological activity.
- International Hemoglobin Information Center
- International Hemoglobin Information Center. Variant list.
- Relative Roles of Heme-Irons and Globin-Thiols in the Genesis of Acellular Hemoglobin Mediated Vasoconstriction
- Nitric oxide, S-nitrosothiols and hemoglobin: is methodology the key?
- Haemoglobin: NO transporter, NO inactivator or NOne of the above?
- Functional properties of the newly observed (G)γ-chain fetal hemoglobin variant Hb F-Monserrato-Sassari (HBG2:c.280T>C) or [(G)γ93 (F9) Cys→Arg].
- A New β Chain Hemoglobin Variant With Increased Oxygen Affinity: Hb Santa Giusta Sardegna [β93(F9)Cys→Trp; HBB c.282T>G]
- Site-directed mutagenesis of cysteine residues alters oxidative stability of fetal hemoglobin
- Human Hemoglobin Genetics
- Erratum to: Unexpectedly low pulse oximetry measurements associated with variant hemoglobins: A systematic review
- Variants of the Alpea Chain
- International Hemoglobin Information Center
- IHIC Variants List
- Three Haemoglobin Variants for Congenital Erythrocytosis and Sickle Cell Disease HbSC
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