FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1574162569> ?p ?o ?g. }

• W1574162569 endingPage "4806" @default.
• W1574162569 startingPage "4800" @default.
• W1574162569 abstract "Abstract Both deoxyhemoglobin (deoxyHb) and carboxyhemoglobin (HbCO) from the lamprey Petromyzon marinus undergo subunit association-dissociation equilibria. By means of sedimentation equilibrium techniques these equilibria were examined at a variety of heme concentrations and at pH values from 4.9 to 8.5. The reactions for deoxyHb are described by the scheme: Hb4 (K4,2)/⇌ 2Hb2 (K2,1)/⇌ 4Hb Both constants are pH dependent above pH 6.0, while below this pH they are essentially invariant and have values of K4,2 = 600 µm and K2,1 = 0.4 µm. The association of single chains to dimers is most simply explained by assuming that protonation of one site per monomer promotes dimer formation: the pK of this site in deoxyHb is calculated to be 6.0. At higher pH the value of K2,1 increases rapidly, and a plot of log K2,1 versus pH is linear with a slope of 2. Aggregation of HbCO and oxyhemoglobin, HbO2, occurs via similar reactions. Below pH 6.0 K'2,1, the dissociation equilibrium constant for HbCO, is essentially invariant with a value of 0.4 mm, and, for this liganded form, the pK of the protonatable group is also estimated to be 6.0. This value of K'2,1 agrees well with the value expected for HbO2 from the linkage requirements of the O2-binding equilibria. Association of HbCO to tetramers also occurs, and at low pH K'4,2 for HbCO is approximately 2 to 3 mm. The calculated values of the association-dissociation equilibrium constants suggest that at pH between 7.0 and 8.0 and at protein concentrations found in the lamprey erythrocyte, deoxyHb will be predominantly dimeric and HbO2 will be predominantly monomeric. Thus, oxygenation in the red cell is accompanied by dissociation. The cooperativity in ligand binding which is exhibited by lamprey hemoglobin can be explained by this linkage between ligation and subunit association-dissociation reactions. Under conditions where these interactions cannot occur, whether in dilute protein solution at alkaline pH or in strong protein solution at acid pH, cooperativity is greatly diminished. Finally, these physical properties of lamprey hemoglobin are used to formulate a model which accounts for the efficient transport of oxygen in vivo by these animals." @default.
• W1574162569 created "2016-06-24" @default.
• W1574162569 creator A5061198942 @default.
• W1574162569 date "1971-08-01" @default.
• W1574162569 modified "2023-10-15" @default.
• W1574162569 title "Sedimentation Equilibrium Experiments on the Self-Association of Hemoglobin from the Lamprey Petromyzon marinus" @default.
• W1574162569 cites W127541880 @default.
• W1574162569 cites W1530231574 @default.
• W1574162569 cites W1596472619 @default.
• W1574162569 cites W1973956782 @default.
• W1574162569 cites W1980547310 @default.
• W1574162569 cites W2002637396 @default.
• W1574162569 cites W2023032254 @default.
• W1574162569 cites W2054591456 @default.
• W1574162569 cites W2070684152 @default.
• W1574162569 cites W2074456757 @default.
• W1574162569 cites W2079210436 @default.
• W1574162569 cites W2109549801 @default.
• W1574162569 cites W2122695744 @default.
• W1574162569 cites W230984257 @default.
• W1574162569 cites W23156506 @default.
• W1574162569 doi "https://doi.org/10.1016/s0021-9258(18)62006-x" @default.
• W1574162569 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/5562359" @default.
• W1574162569 hasPublicationYear "1971" @default.
• W1574162569 type Work @default.
• W1574162569 sameAs 1574162569 @default.
• W1574162569 citedByCount "28" @default.
• W1574162569 countsByYear W15741625692017 @default.
• W1574162569 crossrefType "journal-article" @default.
• W1574162569 hasAuthorship W1574162569A5061198942 @default.
• W1574162569 hasBestOaLocation W15741625691 @default.
• W1574162569 hasConcept C151730666 @default.
• W1574162569 hasConcept C185592680 @default.
• W1574162569 hasConcept C2778917026 @default.
• W1574162569 hasConcept C2780417240 @default.
• W1574162569 hasConcept C2816523 @default.
• W1574162569 hasConcept C2909643359 @default.
• W1574162569 hasConcept C29941650 @default.
• W1574162569 hasConcept C46749446 @default.
• W1574162569 hasConcept C54689828 @default.
• W1574162569 hasConcept C55493867 @default.
• W1574162569 hasConcept C86803240 @default.
• W1574162569 hasConceptScore W1574162569C151730666 @default.
• W1574162569 hasConceptScore W1574162569C185592680 @default.
• W1574162569 hasConceptScore W1574162569C2778917026 @default.
• W1574162569 hasConceptScore W1574162569C2780417240 @default.
• W1574162569 hasConceptScore W1574162569C2816523 @default.
• W1574162569 hasConceptScore W1574162569C2909643359 @default.
• W1574162569 hasConceptScore W1574162569C29941650 @default.
• W1574162569 hasConceptScore W1574162569C46749446 @default.
• W1574162569 hasConceptScore W1574162569C54689828 @default.
• W1574162569 hasConceptScore W1574162569C55493867 @default.
• W1574162569 hasConceptScore W1574162569C86803240 @default.
• W1574162569 hasIssue "15" @default.
• W1574162569 hasLocation W15741625691 @default.
• W1574162569 hasOpenAccess W1574162569 @default.
• W1574162569 hasPrimaryLocation W15741625691 @default.
• W1574162569 hasRelatedWork W1977429703 @default.
• W1574162569 hasRelatedWork W2012509016 @default.
• W1574162569 hasRelatedWork W2013183223 @default.
• W1574162569 hasRelatedWork W2023660866 @default.
• W1574162569 hasRelatedWork W2040068485 @default.
• W1574162569 hasRelatedWork W2052241057 @default.
• W1574162569 hasRelatedWork W2085808239 @default.
• W1574162569 hasRelatedWork W2088975841 @default.
• W1574162569 hasRelatedWork W3117557760 @default.
• W1574162569 hasRelatedWork W3145815143 @default.
• W1574162569 hasVolume "246" @default.
• W1574162569 isParatext "false" @default.
• W1574162569 isRetracted "false" @default.
• W1574162569 magId "1574162569" @default.
• W1574162569 workType "article" @default.