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Studies on the mechanism of action of cyanate in sickle cell disease. Oxygen affinity and gelling properties of hemoglobin S carbamylated on specific chains.

AuthorsA M Nigen, N Njikam, C K Lee, J M Manning
JournalThe Journal of biological chemistry (J Biol Chem) Vol. 249 Issue 20 Pg. 6611-6 (Oct 25 1974) ISSN: 0021-9258 [Print] United States
PMID4421180 (Publication Type: Comparative Study, Journal Article)
Chemical References
  • Carbamates
  • Cyanates
  • Gels
  • Hemoglobin, Sickle
  • Hemoglobins, Abnormal
  • Hydroxymercuribenzoates
  • Macromolecular Substances
  • Oxyhemoglobins
  • Mercaptoethanol
  • Carboxyhemoglobin
  • Oxygen
Topics
  • Anemia, Sickle Cell (blood)
  • Binding Sites
  • Blood Protein Electrophoresis
  • Carbamates
  • Carboxyhemoglobin
  • Chromatography, DEAE-Cellulose
  • Chromatography, Ion Exchange
  • Cyanates
  • Electrophoresis, Polyacrylamide Gel
  • Gels
  • Hemoglobin, Sickle
  • Hemoglobins, Abnormal
  • Humans
  • Hydrogen-Ion Concentration
  • Hydroxymercuribenzoates
  • Kinetics
  • Macromolecular Substances
  • Mercaptoethanol
  • Oxygen (blood)
  • Oxyhemoglobins
  • Protein Binding
  • Protein Conformation
  • Spectrophotometry
  • Temperature
  • Time Factors
  • Ultrafiltration

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