Hb-Linköping (beta 36 Pro----Thr): a new hemoglobin mutant characterized by reversed-phase high-performance liquid chromatography.

Preparative separation of alpha- and beta-chains from a newly identified abnormal hemoglobin has been performed on a new C1/C8 column. Tryptic peptides from the abnormal beta-chain were subjected to peptide mapping on a new C2/C18 column with a reversed-phase system including potassium dihydrogen phosphate (pH 2.9) as a hydrophilic ion-pairing reagent. A hydrophobic substitution, beta 36 proline-threonine, was evident after amino acid analysis and Edman degradation of the isolated mutant peptide. Replacement of proline as the second amino acid in the C-helix represents an important structural change in the alpha 1 beta 2-contact.