| pubmed-article:3841063 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3841063 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:3841063 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:3841063 | lifeskim:mentions | umls-concept:C1979845 | lld:lifeskim |
| pubmed-article:3841063 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:3841063 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:3841063 | lifeskim:mentions | umls-concept:C0313479 | lld:lifeskim |
| pubmed-article:3841063 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:3841063 | pubmed:dateCreated | 1986-2-13 | lld:pubmed |
| pubmed-article:3841063 | 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. | lld:pubmed |
| pubmed-article:3841063 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3841063 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3841063 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3841063 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3841063 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3841063 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3841063 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3841063 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3841063 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3841063 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:3841063 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:3841063 | pubmed:author | pubmed-author:BardakdjianJJ | lld:pubmed |
| pubmed-article:3841063 | pubmed:author | pubmed-author:PoyartCC | lld:pubmed |
| pubmed-article:3841063 | pubmed:author | pubmed-author:RosaJJ | lld:pubmed |
| pubmed-article:3841063 | pubmed:author | pubmed-author:BlouquitYY | lld:pubmed |
| pubmed-article:3841063 | pubmed:author | pubmed-author:LacombeCC | lld:pubmed |
| pubmed-article:3841063 | pubmed:author | pubmed-author:RiouJJ | lld:pubmed |
| pubmed-article:3841063 | pubmed:author | pubmed-author:ArousNN | lld:pubmed |
| pubmed-article:3841063 | pubmed:author | pubmed-author:CraescuC TCT | lld:pubmed |
| pubmed-article:3841063 | pubmed:author | pubmed-author:KisterJJ | lld:pubmed |
| pubmed-article:3841063 | pubmed:author | pubmed-author:Delanoe-Garin... | lld:pubmed |
| pubmed-article:3841063 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3841063 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:3841063 | pubmed:volume | 153 | lld:pubmed |
| pubmed-article:3841063 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3841063 | pubmed:authorsComplete | N | lld:pubmed |
| pubmed-article:3841063 | pubmed:pagination | 655-62 | lld:pubmed |
| pubmed-article:3841063 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:3841063 | pubmed:meshHeading | pubmed-meshheading:3841063-... | lld:pubmed |
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| pubmed-article:3841063 | pubmed:meshHeading | pubmed-meshheading:3841063-... | lld:pubmed |
| pubmed-article:3841063 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:3841063 | pubmed:articleTitle | Structural and functional studies of hemoglobin Poissy alpha 2 beta 2(56) (D7) Gly----Arg and 86 (F2) Ala----Pro. | lld:pubmed |
| pubmed-article:3841063 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3841063 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3841063 | lld:pubmed |
