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.
D000596:Amino Acids / Q000032:analysis*; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D006455:Hemoglobins, Abnormal / Q000032:analysis* / Q000235:genetics; D006801:Humans; D006868:Hydrolysis; D007525:Isoelectric Focusing; D009154:Mutation; D010455:Peptides / Q000032:analysis; D014357:Trypsin
D000596:Amino Acids; D006455:Hemoglobins, Abnormal; D010455:Peptides; C042854:hemoglobin Linkoeping; D014357:Trypsin