title: 1H-n.m.r. and c.d. studies of haem orientational disorder in sperm-whale myoglobin and human haemoglobin.
abstract: 1H-n.m.r. and c.d. studies on sperm-whale myoglobin show that the c.d. signal in the Soret region is inversely and linearly related to the proportion of minor isomer present. An alternative method, 'pH jump', is described for inducing orientational disorder in sperm-whale myoglobin without recourse to reconstitution. 1H-n.m.r. studies on human haemoglobin A indicate little heterogeneity in freshly isolated haemoglobin A, but the effect is enhanced in freeze-dried Sigma haemoglobin A.
authors.affiliation: Department of Chemistry, University of Essex, Wivenhoe Park, Colchester, U.K.
authors.forename: H S
authors.initials: HS
authors.lastname: Aojula
authors.forename: M T
authors.initials: MT
authors.lastname: Wilson
authors.forename: G R
authors.initials: GR
authors.lastname: Moore
authors.forename: D J
authors.initials: DJ
authors.lastname: Williamson
mesh_terms: D000818:Animals; D002942:Circular Dichroism; D006418:Heme / Q000032:analysis*; D006441:Hemoglobin A; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D009211:Myoglobin; D014907:Whales
chemical_list: D009211:Myoglobin; D006418:Heme; D006441:Hemoglobin A