Pratumtip BoontrakoonpoontaweeJisnuson SvastiSuthat FucharoenPranee WinichagoonMahidol UniversityFaculty of Medicine, Siriraj Hospital, Mahidol University2018-06-142018-06-141987-01-01Hemoglobin. Vol.11, No.4 (1987), 309-316036302692-s2.0-0023220619https://repository.li.mahidol.ac.th/handle/20.500.14594/15326The proposita was a Thai female showing signs of a mild anemia (Hb: 11.4 g/dl; RBC: 4.91 × 10 6 /mm 3 ; reticulocytes: 2.4%; MCV: 70 fl; MCHC: 23.3 g/dl). Hemoglobins were isolated by DEAE-cellulose chromatography in the following relative amounts: Hb E + Hb A 2 = 53%; Hb F 0 = 30.0%; Hb δbeta;Lepore = 12.7%; Hb F 1 = 4.3% The β E and δbeta;Lepore chains were isolated by CM-cellulose chromatography and were subjected to tryptic peptide mapping on paper in comparison to normal β A chains. Amino acid analysis of selected peptides permitted unambiguous identification of the abnormal hemoglobins as Hb E [β26(B8)GluLys] and Hb Lepore-Washington-Boston, which has a δ chain sequence for residues 1-87, and a β chain sequence for residues 116-146. The presence of a Lepore hemoglobin was further confirmed by Pst I digestion of the proposita's DNA. The association of the two hemoglobin variants gave rise to elevated levels of Hb F. © 1987 Informa UK Ltd All rights reserved: reproduction in whole or part not permitted.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyMedicineArticleSCOPUS10.3109/03630268709042850