Abstract |
It was previously reported that Hb Philly with a mutation of Phe for Tyr at 35(C1)beta showed non-cooperative oxygen binding with a very high affinity and instability leading to hemolysis. Further, it lacked the 1H-NMR signal at 13.1 ppm from 2,2-dimethyl-2-silapentane-5-sulfonate in normal hemoglobin (Hb A), so that this signal was assigned to a hydrogen bond formed by Tyr-35(C1)beta. Surprisingly, our artificial mutant hemoglobin with the same mutation as Hb Philly showed slightly lowered oxygen affinity, almost normal cooperativity, the 1H-NMR signal at 13.1 ppm and no sign of instability. Our results indicate that the mutation reported for Hb Philly and the assignment of the 13.1 ppm signal need reexamination.
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Authors | T Nakatsukasa, N Nomura, G Miyazaki, K Imai, Y Wada, K Ishimori, I Morishima, H Morimoto |
Journal | FEBS letters
(FEBS Lett)
Vol. 441
Issue 1
Pg. 93-6
(Dec 11 1998)
ISSN: 0014-5793 [Print] England |
PMID | 9877172
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Hemoglobins
- Macromolecular Substances
- Oxyhemoglobins
- Recombinant Proteins
- Tyrosine
- Phenylalanine
- Globins
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Topics |
- Amino Acid Substitution
- Binding Sites
- Globins
(chemistry)
- Hemoglobins
(chemistry, metabolism)
- Humans
- Hydrogen Bonding
- Kinetics
- Macromolecular Substances
- Mutagenesis, Site-Directed
- Nuclear Magnetic Resonance, Biomolecular
- Oxyhemoglobins
(chemistry, metabolism)
- Phenylalanine
- Point Mutation
- Protein Conformation
- Recombinant Proteins
(chemistry)
- Tyrosine
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