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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1998-4-16
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pubmed:abstractText |
Hb Godavari [alpha 95(G2)Pro-->Thr] was characterized independently in two families of different ethnic origin. The first case, found in the Netherlands, involved an Indian patient. The second one was identified a few months later in an African family from Mali, living in France. Hb Godavari is the fourth example of a substitution involving neutral residues at position alpha 95(G2). In all these variants the electrophoretic pattern suggested that the structural modification unmasks a charged residue buried in the alpha 1 beta 2 contact area. The oxygen affinity of this abnormal hemoglobin was approximately 10% higher than that of Hb A; in the absence of 2,3-diphosphoglycerate, its cooperativity was moderately decreased, suggesting a slightly unstable T state.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0363-0269
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11-22
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:9494044-Adult,
pubmed-meshheading:9494044-Amino Acid Substitution,
pubmed-meshheading:9494044-Child, Preschool,
pubmed-meshheading:9494044-Electrophoresis, Agar Gel,
pubmed-meshheading:9494044-Electrophoresis, Cellulose Acetate,
pubmed-meshheading:9494044-Female,
pubmed-meshheading:9494044-Hemoglobins, Abnormal,
pubmed-meshheading:9494044-Humans,
pubmed-meshheading:9494044-Infant,
pubmed-meshheading:9494044-Isoelectric Focusing,
pubmed-meshheading:9494044-Male,
pubmed-meshheading:9494044-Oxygen,
pubmed-meshheading:9494044-Pedigree,
pubmed-meshheading:9494044-Point Mutation,
pubmed-meshheading:9494044-Proline,
pubmed-meshheading:9494044-Threonine
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pubmed:year |
1998
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pubmed:articleTitle |
Hb Godavari [alpha 95(G2)Pro-->Thr]: a neutral amino acid substitution in the alpha 1 beta 2 interface that modifies the electrophoretic mobility of hemoglobin.
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pubmed:affiliation |
INSERM U91 and Department of Biochemistry, Hôpital Henri Mondor, Créteil, France.
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pubmed:publicationType |
Journal Article,
Case Reports
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