| Original language | English (US) |
|---|---|
| Pages (from-to) | 220-222 |
| Number of pages | 3 |
| Journal | BBA - Protein Structure |
| Volume | 154 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 22 1968 |
ASJC Scopus subject areas
- General Medicine
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In: BBA - Protein Structure, Vol. 154, No. 1, 22.01.1968, p. 220-222.
Research output: Contribution to journal › Article › peer-review
}
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
UR - http://www.scopus.com/inward/record.url?scp=0014426230&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0014426230&partnerID=8YFLogxK
U2 - 10.1016/0005-2795(68)90274-2
DO - 10.1016/0005-2795(68)90274-2
M3 - Article
C2 - 5639009
AN - SCOPUS:0014426230
SN - 0005-2795
VL - 154
SP - 220
EP - 222
JO - BBA - Protein Structure
JF - BBA - Protein Structure
IS - 1
ER -