Linked Life Data

11673898

Source:http://linkedlifedata.com/resource/pubmed/id/11673898

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-10-24
pubmed:abstractText
Formation of the asymmetric hemoglobin hybrid FS (alpha2gammabetaS) inhibits hemoglobin S (Hb S) polymerization in vitro and underlies the protective effect of fetal hemoglobin (Hb F) in homozygous sickle cell disease. Conventional methods for separating Hb reveal only symmetric Hb tetramers because of the rapid dissociation of tetramers to dimers relative to the separation time for electrophoresis and chromatography. To gain insight into the quantitative distribution of asymmetric Hb FS and other tetrameric species in sickle cell disease, the noncovalent association of Hb subunits in hemolysates was studied by a novel application of electrospray ionization mass spectrometry (ESI-MS). Mass spectra of both patient and fetal blood revealed predominance of tetrameric species with dimer and monomer subunits in lower abundance. ESI-MS analysis revealed the hybrid Hb AF (alpha2gammabetaA) in hemolysates shown by conventional high-performance liquid chromatography to contain only the symmetric species Hb A (alpha2betaA2) and Hb F (alpha2gamma2). A unique tetramer of average mass 64,558 Da was identified in hemolysates from patients with sickle cell disease in accordance with the calculated mass of the asymmetric Hb hybrid FS. Hybrid Hb species were stable under the ESI-MS conditions employed allowing concurrent determination of the proportions of Hb FS and the symmetrical Hb S (alpha2betaS2). The ratios of Hb FS to Hb S correlated closely (r2 = 0.96) with those predicted under physiological conditions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0003-2697
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
298
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
76-82
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Mass spectral analysis of asymmetric hemoglobin hybrids: demonstration of Hb FS (alpha2gammabetaS) in sickle cell disease.
pubmed:affiliation
Department of Haematological Medicine, Guy's, King's, and St Thomas' School of Medicine, Denmark Hill, London, SE5 9RS, United Kingdom. soforia@usamail.usouthal.edu
pubmed:publicationType
Journal Article, Clinical Trial, Research Support, Non-U.S. Gov't