HB Cleveland or α2β293(f9)CYS→ARG;121(GH4)GLU→GLN

J. B. Wilson; M. Ramachandran; B. B. Webber; F. Kutlar; L. F. Hazelnood; D. Barnett; N. V. Hirschler; T. H.J. Huisman

doi:10.3109/03630269109027879

HB Cleveland or α₂β₂93(f9)CYS→ARG;121(GH4)GLU→GLN

J. B. Wilson, M. Ramachandran, B. B. Webber, F. Kutlar, L. F. Hazelnood, D. Barnett, N. V. Hirschler, T. H.J. Huisman

Pulmonary Disease

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

9 Scopus citations

Abstract

Hb Cleveland is characterized by two amino acid Substitutions, namely β121(GH4)Glu→Gln as in Hb D-Los Angeles and β93(F9)Cys→Arg as in Hb Okazaki, and shares with Hb Okazaki a decreased stability, an increase in oxygen affinity, and decreases in Bohr effect and heme-heme interaction. It is the 13th β chain variant with two substitutions that has been described thus far.

Original language	English (US)
Pages (from-to)	269-278
Number of pages	10
Journal	Hemoglobin
Volume	15
Issue number	4
DOIs	https://doi.org/10.3109/03630269109027879
State	Published - 1991

ASJC Scopus subject areas

Hematology
Genetics(clinical)
Clinical Biochemistry
Biochemistry, medical

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@article{8b1bfe217bfe44189070139525974f5b,

title = "HB Cleveland or α2β293(f9)CYS→ARG;121(GH4)GLU→GLN",

abstract = "Hb Cleveland is characterized by two amino acid Substitutions, namely β121(GH4)Glu→Gln as in Hb D-Los Angeles and β93(F9)Cys→Arg as in Hb Okazaki, and shares with Hb Okazaki a decreased stability, an increase in oxygen affinity, and decreases in Bohr effect and heme-heme interaction. It is the 13th β chain variant with two substitutions that has been described thus far.",

author = "Wilson, {J. B.} and M. Ramachandran and Webber, {B. B.} and F. Kutlar and Hazelnood, {L. F.} and D. Barnett and Hirschler, {N. V.} and Huisman, {T. H.J.}",

note = "Funding Information: This research was supported by USPHS Research Grant HLB-05168. This is contribution #1285 from the Department of Cell and Molecular Biology at the Medical College of Georgia in Augusta, Georgia.",

year = "1991",

doi = "10.3109/03630269109027879",

language = "English (US)",

volume = "15",

pages = "269--278",

journal = "Hemoglobin",

issn = "0363-0269",

publisher = "Informa Healthcare",

number = "4",

}

TY - JOUR

T1 - HB Cleveland or α2β293(f9)CYS→ARG;121(GH4)GLU→GLN

AU - Wilson, J. B.

AU - Ramachandran, M.

AU - Webber, B. B.

AU - Kutlar, F.

AU - Hazelnood, L. F.

AU - Barnett, D.

AU - Hirschler, N. V.

AU - Huisman, T. H.J.

N1 - Funding Information: This research was supported by USPHS Research Grant HLB-05168. This is contribution #1285 from the Department of Cell and Molecular Biology at the Medical College of Georgia in Augusta, Georgia.

PY - 1991

Y1 - 1991

N2 - Hb Cleveland is characterized by two amino acid Substitutions, namely β121(GH4)Glu→Gln as in Hb D-Los Angeles and β93(F9)Cys→Arg as in Hb Okazaki, and shares with Hb Okazaki a decreased stability, an increase in oxygen affinity, and decreases in Bohr effect and heme-heme interaction. It is the 13th β chain variant with two substitutions that has been described thus far.

AB - Hb Cleveland is characterized by two amino acid Substitutions, namely β121(GH4)Glu→Gln as in Hb D-Los Angeles and β93(F9)Cys→Arg as in Hb Okazaki, and shares with Hb Okazaki a decreased stability, an increase in oxygen affinity, and decreases in Bohr effect and heme-heme interaction. It is the 13th β chain variant with two substitutions that has been described thus far.

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U2 - 10.3109/03630269109027879

DO - 10.3109/03630269109027879

M3 - Article

C2 - 1787096

AN - SCOPUS:0025830709

VL - 15

SP - 269

EP - 278

JO - Hemoglobin

JF - Hemoglobin

SN - 0363-0269

IS - 4