Studies on the mechanism of action of cyanate in sickle cell disease. Oxygen affinity and gelling properties of hemoglobin S carbamylated on specific chains.
D000755:Anemia, Sickle Cell / Q000097:blood*; D001665:Binding Sites; D001797:Blood Protein Electrophoresis; D002219:Carbamates; D002263:Carboxyhemoglobin; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D003485:Cyanates; D004591:Electrophoresis, Polyacrylamide Gel; D005782:Gels; D006451:Hemoglobin, Sickle; D006455:Hemoglobins, Abnormal; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006902:Hydroxymercuribenzoates; D007700:Kinetics; D046911:Macromolecular Substances; D008623:Mercaptoethanol; D010100:Oxygen / Q000097:blood*; D010108:Oxyhemoglobins; D011485:Protein Binding; D011487:Protein Conformation; D013053:Spectrophotometry; D013696:Temperature; D013997:Time Factors; D014462:Ultrafiltration
D002219:Carbamates; D003485:Cyanates; D005782:Gels; D006451:Hemoglobin, Sickle; D006455:Hemoglobins, Abnormal; D006902:Hydroxymercuribenzoates; D046911:Macromolecular Substances; D010108:Oxyhemoglobins; D008623:Mercaptoethanol; D002263:Carboxyhemoglobin; D010100:Oxygen