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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1986-2-13
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pubmed:abstractText |
Hemoglobin Poissy alpha 2 beta 2(56) (D7) Gly----Arg and 86 (F2) Ala----Pro, is a new variant of the beta chain with two substitutions within the second exon of the corresponding gene. The electrophoretic mobilities are identical to those of Hb Hamadan alpha 2 beta 2(56) (D7) Gly----Arg as is the fingerprint of the tryptic hydrolysate of the two abnormal beta chains. The second substitution beta 86 Ala----Pro was detected by high-pressure liquid chromatography. Hb Poissy has a threefold increase in oxygen affinity with low Hill coefficient and diminished Bohr effect, which are restored to normal upon addition of 2,3-bisphosphoglycerate. Since the functional properties of Hb Hamadan (beta 56 Gly----Arg) have been described as normal, the abnormal function of Hb Poissy may be attributed to the beta 86 (F2) Ala----Pro substitution. Hb Poissy exhibits a mild instability and a greater reactivity of the thiol groups of the beta 93 (F9) Cys residues in the deoxy form than does Hb A. The oxidation rate of Hb Poissy is biphasic indicating a large inequivalence between the alpha and beta hemes. Thereafter NMR studies demonstrated that the beta 86 Ala----Pro substitution produces a displacement of the F helix closer to the heme plane and a large increase in the dynamic fluctuations of the tertiary structure on the proximal side of the beta hemes. These results lead to the conclusion that the beta 86 Ala----Pro substitution produces a destabilization of the F helix extending downwards to the FG corner and altering both the beta hemes and the alpha 1 beta 2 contacts.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Hemoglobins, Abnormal,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Compounds
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
153
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pubmed:owner |
NLM
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pubmed:authorsComplete |
N
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pubmed:pagination |
655-62
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:3841063-Amino Acids,
pubmed-meshheading:3841063-Chemical Phenomena,
pubmed-meshheading:3841063-Chemistry,
pubmed-meshheading:3841063-Chromatography, High Pressure Liquid,
pubmed-meshheading:3841063-DNA,
pubmed-meshheading:3841063-Hemoglobins, Abnormal,
pubmed-meshheading:3841063-Humans,
pubmed-meshheading:3841063-Isoelectric Focusing,
pubmed-meshheading:3841063-Magnetic Resonance Spectroscopy,
pubmed-meshheading:3841063-Male,
pubmed-meshheading:3841063-Middle Aged,
pubmed-meshheading:3841063-Oxidation-Reduction,
pubmed-meshheading:3841063-Oxygen,
pubmed-meshheading:3841063-Sulfhydryl Compounds
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pubmed:year |
1985
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pubmed:articleTitle |
Structural and functional studies of hemoglobin Poissy alpha 2 beta 2(56) (D7) Gly----Arg and 86 (F2) Ala----Pro.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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