HemoglobinBibba or α2136Pro β2, an unstable α chain abnormal hemoglobin

Enno F. Kleihauer; Cecelia A. Reynolds; Andrée M. Dozy; Jerry B. Wilson; Russell R. Moores; M. P. Berenson; Claude Starr Wright; Titus H.J. Huisman

doi:10.1016/0005-2795(68)90274-2

Hemoglobin_Bibba or α₂^136Pro β₂, an unstable α chain abnormal hemoglobin

Enno F. Kleihauer, Cecelia A. Reynolds, Andrée M. Dozy, Jerry B. Wilson, Russell R. Moores, M. P. Berenson, Claude Starr Wright, Titus H.J. Huisman

Pulmonary Disease

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47 Scopus citations

Original language	English (US)
Pages (from-to)	220-222
Number of pages	3
Journal	BBA - Protein Structure
Volume	154
Issue number	1
DOIs	https://doi.org/10.1016/0005-2795(68)90274-2
State	Published - Jan 22 1968

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Medicine(all)

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10.1016/0005-2795(68)90274-2

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@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",

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publisher = "Elsevier",

number = "1",

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TY - JOUR

T1 - HemoglobinBibba or α2136Pro β2, an unstable α chain abnormal hemoglobin

AU - Kleihauer, Enno F.

AU - Reynolds, Cecelia A.

AU - Dozy, Andrée M.

AU - Wilson, Jerry B.

AU - Moores, Russell R.

AU - Berenson, M. P.

AU - Wright, Claude Starr

AU - Huisman, Titus H.J.

N1 - 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.

PY - 1968/1/22

Y1 - 1968/1/22

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U2 - 10.1016/0005-2795(68)90274-2

DO - 10.1016/0005-2795(68)90274-2

M3 - Article

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AN - SCOPUS:0014426230

SN - 0005-2795

VL - 154

SP - 220

EP - 222

JO - BBA - Protein Structure

JF - BBA - Protein Structure

IS - 1

ER -

HemoglobinBibba or α2136Pro β2, an unstable α chain abnormal hemoglobin

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Hemoglobin_Bibba or α₂^136Pro β₂, an unstable α chain abnormal hemoglobin