Net charge and oxygen affinity of human hemoglobin are independent of hemoglobin concentration

Gerolf Gros, Harry S. Rollema, Wolfgang Jelkmann, Hanne Gros, Christian Bauer, Waldemar Moll

12 Zitate (Scopus)

Abstract

The dependence of net charge and oxygen affinity of human hemoglobin upon hemoglobin concentration was reinvestigated. In contrast to earlier reports from various laboratories, both functional properties of hemoglobin were found to be independent of hemoglobin concentration. Two findings indicate a concentration-independent net charge of carbonmonoxy hemoglobin at pH 6.6: (a) the pH value of a given carbonmonoxy hemoglobin solution remains constant at 6.6 when the hemoglobin concentration is raised from 10 to 40 g/dl, indicating that there is no change in protonation of titratable groups of hemoglobin; (b) the net charge of carbonmonoxy hemoglobin as estimated from the Donnan distribution of 22Na+ shows no dependence on hemoglobin concentration in this concentration range. The oxygen affinity of human hemoglobin was determined from measurements of oxygen concentrations in equilibrated samples using a Lex-O2- Con apparatus (Lexington Instruments, Waltham, Mass.). P50 averaged 11.4 mm Hg at 37°C, pH = 7.2, and ionic strength ≈ 0.15. Neither P50 nor Hill’s w showed any variation with hemoglobin concentrations increasing from 10 to 40 g/dl.

OriginalspracheEnglisch
ZeitschriftJournal of General Physiology
Jahrgang72
Ausgabenummer6
Seiten (von - bis)765-773
Seitenumfang9
ISSN0022-1295
DOIs
PublikationsstatusVeröffentlicht - 01.12.1978

Strategische Forschungsbereiche und Zentren

  • Forschungsschwerpunkt: Gehirn, Hormone, Verhalten - Center for Brain, Behavior and Metabolism (CBBM)

Fingerprint

Untersuchen Sie die Forschungsthemen von „Net charge and oxygen affinity of human hemoglobin are independent of hemoglobin concentration“. Zusammen bilden sie einen einzigartigen Fingerprint.

Zitieren