| http://purl.uniprot.org/citations/22298770 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22298770 | http://www.w3.org/2000/01/rdf-schema#comment | "Human α-hemoglobin stabilizing protein (AHSP) is a conserved mammalian erythroid protein that facilitates the production of Hemoglobin A by stabilizing free α-globin. AHSP rapidly binds to ferrous α with association (k'(AHSP)) and dissociation (k(AHSP)) rate constants of ≈10 μm(-1) s(-1) and 0.2 s(-1), respectively, at pH 7.4 at 22 °C. A small slow phase was observed when AHSP binds to excess ferrous αCO. This slow phase appears to be due to cis to trans prolyl isomerization of the Asp(29)-Pro(30) peptide bond in wild-type AHSP because it was absent when αCO was mixed with P30A and P30W AHSP, which are fixed in the trans conformation. This slow phase was also absent when met(Fe(3+))-α reacted with wild-type AHSP, suggesting that met-α is capable of rapidly binding to either Pro(30) conformer. Both wild-type and Pro(30)-substituted AHSPs drive the formation of a met-α hemichrome conformation following binding to either met- or oxy(Fe(2+))-α. The dissociation rate of the met-α·AHSP complex (k(AHSP) ≈ 0.002 s(-1)) is ∼100-fold slower than that for ferrous α·AHSP complexes, resulting in a much higher affinity of AHSP for met-α. Thus, in vivo, AHSP acts as a molecular chaperone by rapidly binding and stabilizing met-α hemichrome folding intermediates. The low rate of met-α dissociation also allows AHSP to have a quality control function by kinetically trapping ferric α and preventing its incorporation into less stable mixed valence Hemoglobin A tetramers. Reduction of AHSP-bound met-α allows more rapid release to β subunits to form stable fully, reduced hemoglobin dimers and tetramers."xsd:string |
| http://purl.uniprot.org/citations/22298770 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m111.313247"xsd:string |
| http://purl.uniprot.org/citations/22298770 | http://purl.uniprot.org/core/author | "Weiss M.J."xsd:string |
| http://purl.uniprot.org/citations/22298770 | http://purl.uniprot.org/core/author | "Olson J.S."xsd:string |
| http://purl.uniprot.org/citations/22298770 | http://purl.uniprot.org/core/author | "Khandros E."xsd:string |
| http://purl.uniprot.org/citations/22298770 | http://purl.uniprot.org/core/author | "Mollan T.L."xsd:string |
| http://purl.uniprot.org/citations/22298770 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22298770 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/22298770 | http://purl.uniprot.org/core/pages | "11338-11350"xsd:string |
| http://purl.uniprot.org/citations/22298770 | http://purl.uniprot.org/core/title | "Kinetics of alpha-globin binding to alpha-hemoglobin stabilizing protein (AHSP) indicate preferential stabilization of hemichrome folding intermediate."xsd:string |
| http://purl.uniprot.org/citations/22298770 | http://purl.uniprot.org/core/volume | "287"xsd:string |
| http://purl.uniprot.org/citations/22298770 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22298770 |
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| http://purl.uniprot.org/uniprot/#_Q9NZD4-mappedCitation-22298770 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/22298770 |
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