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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1981-5-13
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pubmed:abstractText |
Hemoglobin Hotel-Dieu was detected by isoelectric focusing during investigation of a patient who had erythrocytosis. This variant migrates on cellulose acetate electrophoresis to a cathodic position relative to Hb F. In hemoglobin Hotel-Dieu, aspartic acid is substituted by glycine in position 99 of the beta chain. As in other abnormal hemoglobins in which substitution of this residue has occurred, Hb Hotel-Dieu exhibits a high oxygen affinity and is associated with familial erythrocytosis.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
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pubmed:status |
MEDLINE
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pubmed:issn |
0363-0269
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
19-31
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7204092-Adult,
pubmed-meshheading:7204092-Amino Acids,
pubmed-meshheading:7204092-Female,
pubmed-meshheading:7204092-Genetic Variation,
pubmed-meshheading:7204092-Hemoglobins,
pubmed-meshheading:7204092-Hemoglobins, Abnormal,
pubmed-meshheading:7204092-Humans,
pubmed-meshheading:7204092-Male,
pubmed-meshheading:7204092-Oxygen,
pubmed-meshheading:7204092-Pedigree,
pubmed-meshheading:7204092-Peptide Fragments,
pubmed-meshheading:7204092-Polycythemia
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pubmed:year |
1981
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pubmed:articleTitle |
Hemoglobin Hotel-Dieu beta 99 Asp replaced by Gly (g1). A new abnormal hemoglobin with high oxygen affinity.
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pubmed:publicationType |
Journal Article,
Case Reports,
Research Support, Non-U.S. Gov't
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