Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-1-27
pubmed:abstractText
The relationship between different amino acids at the beta 6 position of hemoglobin and tetramer stability was addressed by a site-directed mutagenesis approach. Precipitation rates during mechanical agitation of oxyhemoglobins with Gln, Ala, Val, Leu and Trp at the beta 6 position increased 2, 5, 13, 21 and 53 times, respectively, compared with that for Hb A. There was a linear relationship between the log of the precipitation rate constant and amino acid hydrophobicity at the beta 6 position, suggesting that enhanced precipitation of oxy Hb S during mechanical agitation results in part from increased hydrophobicity of beta 6 Val. Deoxyhemoglobin solubility increased in the order of beta 6 Ile, Leu, Val, Trp, Gln, Ala and Glu suggesting that hydrophobic interactions between beta 6 Val and the acceptor site of another hemoglobin molecule during deoxy-Hb S polymerization not only depend on hydrophobicity but also on stereospecificity of the amino acid side chain at the beta 6 position. Furthermore, our results indicate that hydrophobic amino acids at the beta 6 position which promote tetramer instability in the oxy form do not necessarily promote polymerization in the deoxy form.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
315
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
47-50
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Effects of beta 6 amino acid hydrophobicity on stability and solubility of hemoglobin tetramers.
pubmed:affiliation
Children's Hospital of Philadelphia, Department of Pediatrics, PA 19104.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.