Abstract
Structural analysis of a fast-moving hemoglobin variant, present in three members of a Qatari family, identified a Val → Glu substitution at position 1 (NA1) of the β-chain. The introduction of this glutamic acid residue prevents the removal of the initiator methione, thus extending the N-terminus by one residue to Met-Glu-His-Leu-Thr-. THe methionine residue is blocked by an as yet not completely identified molecule. The presence of the variant in a heterozygote does not have clinical consequences.
Original language | English (US) |
---|---|
Pages (from-to) | 257-260 |
Number of pages | 4 |
Journal | Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular |
Volume | 831 |
Issue number | 2 |
DOIs | |
State | Published - Oct 4 1985 |
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Keywords
- (Human)
- Amino acid sequence
- Blocking group
- Hemoglobin variant
- Methionine
- N-terminal
ASJC Scopus subject areas
- Structural Biology
- Biophysics
- Biochemistry
- Molecular Biology
Cite this
Hb Doha or α2β2[X-N-Met-1-(NA1)Val → Glu]; a new β-chain abnormal hemoglobin observed in a Qatari female. / Kamel, K.; El-Najjar, A.; Webber, B. B.; Chen, S. S.; Wilson, J. B.; Kutlar, Abdullah; Huisman, T. H.J.
In: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, Vol. 831, No. 2, 04.10.1985, p. 257-260.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Hb Doha or α2β2[X-N-Met-1-(NA1)Val → Glu]; a new β-chain abnormal hemoglobin observed in a Qatari female
AU - Kamel, K.
AU - El-Najjar, A.
AU - Webber, B. B.
AU - Chen, S. S.
AU - Wilson, J. B.
AU - Kutlar, Abdullah
AU - Huisman, T. H.J.
PY - 1985/10/4
Y1 - 1985/10/4
N2 - Structural analysis of a fast-moving hemoglobin variant, present in three members of a Qatari family, identified a Val → Glu substitution at position 1 (NA1) of the β-chain. The introduction of this glutamic acid residue prevents the removal of the initiator methione, thus extending the N-terminus by one residue to Met-Glu-His-Leu-Thr-. THe methionine residue is blocked by an as yet not completely identified molecule. The presence of the variant in a heterozygote does not have clinical consequences.
AB - Structural analysis of a fast-moving hemoglobin variant, present in three members of a Qatari family, identified a Val → Glu substitution at position 1 (NA1) of the β-chain. The introduction of this glutamic acid residue prevents the removal of the initiator methione, thus extending the N-terminus by one residue to Met-Glu-His-Leu-Thr-. THe methionine residue is blocked by an as yet not completely identified molecule. The presence of the variant in a heterozygote does not have clinical consequences.
KW - (Human)
KW - Amino acid sequence
KW - Blocking group
KW - Hemoglobin variant
KW - Methionine
KW - N-terminal
UR - http://www.scopus.com/inward/record.url?scp=0021931068&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0021931068&partnerID=8YFLogxK
U2 - 10.1016/0167-4838(85)90043-3
DO - 10.1016/0167-4838(85)90043-3
M3 - Article
C2 - 3840039
AN - SCOPUS:0021931068
VL - 831
SP - 257
EP - 260
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
SN - 1570-9639
IS - 2
ER -