@article{cdd9c8c434974e8d83d00acbe5c2a8c4,
title = "HemoglobinBibba or α2136Pro β2, an unstable α chain abnormal hemoglobin",
author = "Kleihauer, {Enno F.} and Reynolds, {Cecelia A.} and Dozy, {Andr{\'e}e M.} and Wilson, {Jerry B.} and Moores, {Russell R.} and Berenson, {M. P.} and Wright, {Claude Starr} and Huisman, {Titus H.J.}",
note = "Funding Information: lyze the peptide bond between tile residues in position 136 and 137 (threonine) as is observed in the aT-I3 peptide of normal Hb-A. The replacement of leucine in position 136 of the a chain by proline has a profound influence on the stability of the abnormal hemoglobin. The substitution occurs in the C-terminal part of the H helix of the a chain and will likely disrupt the helix and change its direction, while as a result the interaction of the a and \[3 chains within the hemoglobin molecule may also be altered. Such a change in tertiary structure is also implicated by the differences in electrophoretic and chromatographic mobilities of the Hb-A and I-IbBibba, which are likely due to a change in the over all charge of the hemoglobin molecule and not to a substitution of an amino acid residue by another carrying a different charge. In this respect HbBibba differs from HbGenova (a2f122sLeu-~Pr°) which has an electrophoretic mobility similar to that of Hb-A, and resembles HbK~sln (a2f1298Val ~Met). This study was supported by U.S. Public Health Service grants HE-o5168 and FR-ooo6I-O5. E.F.K. was supported by U.S. Public Health Service grant i FOS-TW-II27-oI as an International Research Fellow and was on leave from the Department of Pediatrics, University of Munich, Germany.",
year = "1968",
month = jan,
day = "22",
doi = "10.1016/0005-2795(68)90274-2",
language = "English (US)",
volume = "154",
pages = "220--222",
journal = "BBA - Protein Structure",
issn = "0005-2795",
publisher = "Elsevier",
number = "1",
}