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Hemoglobin aggregation in oxygenated sickle cells studied by carbon‐13 rotating frame spin–lattice relaxation in the presence of an off‐resonance radiofrequency field
Author(s) -
James Thomas L.,
Matthews Roberta,
Matson Gerald B.
Publication year - 1979
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1979.360180713
Subject(s) - chemistry , hemoglobin , nuclear magnetic resonance , resonance (particle physics) , lattice (music) , relaxation (psychology) , electron paramagnetic resonance , analytical chemistry (journal) , atomic physics , organic chemistry , medicine , physics , acoustics
Evidence is presented which shows that hemoglobin S in sickle cells has a tendency to aggregate even in the oxygenated state. The basis for that conclusion is derived from 13 C‐nmr rotating‐frame spin–lattice relaxation studies in the presence of an off‐resonance radiofrequency field in which the carbonyl resonances of hemoglobins in erythrocytes are examined. The experiments indicate that the rotational correlation time of hemoglobin S in oxygenated sickle cells at 38°C is 130 nsec compared to a value of 95 nsec for hemoglobin A in normal erythrocytes at the same temperature and the same mean cell hemoglobin content.