Matches in Wikidata for { <http://www.wikidata.org/entity/Q67541673> ?p ?o ?g. }
Showing items 1 to 41 of
41
with 100 items per page.
- Q67541673 description "article scientifique publié en 1977" @default.
- Q67541673 description "articolo scientifico (pubblicato il 1977)" @default.
- Q67541673 description "artikull shkencor i botuar më 01 janar 1977" @default.
- Q67541673 description "artículu científicu espublizáu en xineru de 1977" @default.
- Q67541673 description "im Januar 1977 veröffentlichter wissenschaftlicher Artikel" @default.
- Q67541673 description "scientific article published on 01 January 1977" @default.
- Q67541673 description "wetenschappelijk artikel" @default.
- Q67541673 description "наукова стаття, опублікована в січні 1977" @default.
- Q67541673 name "Thermodynamic studies on subunit assembly in human hemoglobin. Self-association of oxygenated chains (alphaSH and betaSH): determination of stoichiometries and equilibrium constants as a function of temperature" @default.
- Q67541673 name "Thermodynamic studies on subunit assembly in human hemoglobin. Self-association of oxygenated chains (alphaSH and betaSH): determination of stoichiometries and equilibrium constants as a function of temperature" @default.
- Q67541673 name "Thermodynamic studies on subunit assembly in human hemoglobin. Self-association of oxygenated chains" @default.
- Q67541673 type Item @default.
- Q67541673 label "Thermodynamic studies on subunit assembly in human hemoglobin. Self-association of oxygenated chains (alphaSH and betaSH): determination of stoichiometries and equilibrium constants as a function of temperature" @default.
- Q67541673 label "Thermodynamic studies on subunit assembly in human hemoglobin. Self-association of oxygenated chains (alphaSH and betaSH): determination of stoichiometries and equilibrium constants as a function of temperature" @default.
- Q67541673 label "Thermodynamic studies on subunit assembly in human hemoglobin. Self-association of oxygenated chains" @default.
- Q67541673 prefLabel "Thermodynamic studies on subunit assembly in human hemoglobin. Self-association of oxygenated chains (alphaSH and betaSH): determination of stoichiometries and equilibrium constants as a function of temperature" @default.
- Q67541673 prefLabel "Thermodynamic studies on subunit assembly in human hemoglobin. Self-association of oxygenated chains (alphaSH and betaSH): determination of stoichiometries and equilibrium constants as a function of temperature" @default.
- Q67541673 prefLabel "Thermodynamic studies on subunit assembly in human hemoglobin. Self-association of oxygenated chains" @default.
- Q67541673 P1433 Q67541673-C5E469CE-C8E9-4587-AA6A-F02FC2B41C13 @default.
- Q67541673 P1476 Q67541673-B8033B4E-B9CA-4815-BBAD-A4C97B049392 @default.
- Q67541673 P2093 Q67541673-78EF5834-ED52-468B-BA52-027BEE1AB87F @default.
- Q67541673 P2093 Q67541673-D8F3BFEC-F404-477D-A559-757ACB67C267 @default.
- Q67541673 P304 Q67541673-C60C978F-351C-4444-94AA-CFA1305E31F0 @default.
- Q67541673 P31 Q67541673-96AC3144-1675-4B7A-B43A-FCAB9E33252A @default.
- Q67541673 P407 Q67541673-803825B2-C831-4A21-BC00-EF2372D6A406 @default.
- Q67541673 P433 Q67541673-C316428B-2A99-4674-A586-F3E478CD63E5 @default.
- Q67541673 P478 Q67541673-4ABF52A1-2DA0-4296-873A-CD9BFAC749AA @default.
- Q67541673 P577 Q67541673-3ECA9239-C3D3-45AB-AC37-46BAB48663B3 @default.
- Q67541673 P698 Q67541673-AE80A179-5CF0-43AE-81A1-8CBBD0C7719B @default.
- Q67541673 P698 833131 @default.
- Q67541673 P1433 Q867727 @default.
- Q67541673 P1476 "Thermodynamic studies on subunit assembly in human hemoglobin. Self-association of oxygenated chains (alphaSH and betaSH): determination of stoichiometries and equilibrium constants as a function of temperature" @default.
- Q67541673 P2093 "Ackers GK" @default.
- Q67541673 P2093 "Valdes R Jr" @default.
- Q67541673 P304 "74-81" @default.
- Q67541673 P31 Q13442814 @default.
- Q67541673 P407 Q1860 @default.
- Q67541673 P433 "1" @default.
- Q67541673 P478 "252" @default.
- Q67541673 P577 "1977-01-01T00:00:00Z" @default.
- Q67541673 P698 "833131" @default.