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Über Gewinnung und Eigenschaften von humanem Globin
Author(s) -
Kistler P.,
Buri A.,
Nitschmann Hs.
Publication year - 1953
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19530360517
Subject(s) - chemistry , cleavage (geology) , hydrochloric acid , globin , denaturation (fissile materials) , solubility , heme , hemin , carboxyhemoglobin , hemoglobin , chromatography , nuclear chemistry , inorganic chemistry , biochemistry , organic chemistry , catalysis , enzyme , carbon monoxide , geotechnical engineering , fracture (geology) , engineering
The influence of a range of acid pH values on human oxy‐ and carboxyhemoglobin was thoroughly investigated. Above pH 4 at most a very slow conversion into hemiglobin (in the presence of O 2 ) takes place. Denaturation sets in below pH 4 unmasking approximately 34 proton‐binding groups per mole of oxyhemoglobin. Heme always appears as a cleavage product with the acid‐denaturation, the cleavage becoming more and more quantitative on lowering the pH value. The split‐off heme or hemin can be extracted with acetone which simultaneously precipitates the protein. After reneutralization to pH 7.3, it is soluble in water, the solubility percentage increasing with decreasing pH values of the cleavage process. The extent of renaturation which occurs on neutralization of the hydrochloric acid globin increases with increasing completeness of removal of the pigment. The cleavage velocity of oxy‐ and carboxyhemoglobin at various pH values was spectroscopically measured.