Hb Doha or α2β2[X-N-Met-1-(NA1)Val → Glu]; a new β-chain abnormal hemoglobin observed in a Qatari female

K. Kamel; A. El-Najjar; B. B. Webber; S. S. Chen; J. B. Wilson; A. Kutlar; T. H.J. Huisman

doi:10.1016/0167-4838(85)90043-3

Hb Doha or α₂β₂[X-N-Met-1-(NA1)Val → Glu]; a new β-chain abnormal hemoglobin observed in a Qatari female

K. Kamel, A. El-Najjar, B. B. Webber, S. S. Chen, J. B. Wilson, A. Kutlar, T. H.J. Huisman

Pulmonary Disease

Research output: Contribution to journal › Article › peer-review

15 Scopus citations

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	https://doi.org/10.1016/0167-4838(85)90043-3
State	Published - Oct 4 1985

Keywords

(Human)
Amino acid sequence
Blocking group
Hemoglobin variant
Methionine
N-terminal

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology

Access to Document

10.1016/0167-4838(85)90043-3

Cite this

@article{1c2e2947f2da4bb7b75560d1b4ebe745,

title = "Hb Doha or α2β2[X-N-Met-1-(NA1)Val → Glu]; a new β-chain abnormal hemoglobin observed in a Qatari female",

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.",

keywords = "(Human), Amino acid sequence, Blocking group, Hemoglobin variant, Methionine, N-terminal",

author = "K. Kamel and A. El-Najjar and Webber, {B. B.} and Chen, {S. S.} and Wilson, {J. B.} and A. Kutlar and Huisman, {T. H.J.}",

note = "Funding Information: This research was supported in part by USPHS Research Grants HLB-05168 and HLB-15158. The authors are indebted to Dr. L.B. Hendry and his staff (section of Metabolic and Endocrine Disease, Department of Medicine, Medical College of Georgia) for the initial mass spectroscopic data.",

year = "1985",

month = oct,

day = "4",

doi = "10.1016/0167-4838(85)90043-3",

language = "English (US)",

volume = "831",

pages = "257--260",

journal = "BBA - Protein Structure",

issn = "1570-9639",

publisher = "Elsevier",

number = "2",

}

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, A.

AU - Huisman, T. H.J.

N1 - Funding Information: This research was supported in part by USPHS Research Grants HLB-05168 and HLB-15158. The authors are indebted to Dr. L.B. Hendry and his staff (section of Metabolic and Endocrine Disease, Department of Medicine, Medical College of Georgia) for the initial mass spectroscopic data.

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

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U2 - 10.1016/0167-4838(85)90043-3

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AN - SCOPUS:0021931068

VL - 831

SP - 257

EP - 260

JO - BBA - Protein Structure

JF - BBA - Protein Structure

SN - 1570-9639

IS - 2

ER -