Structural and functional studies of hemoglobin J Cala-bria: beta64 (E8) Gly leads to Asp.
Biochim Biophys Acta
; 492(2): 426-32, 1977 Jun 24.
Article
em En
| MEDLINE
| ID: mdl-884140
ABSTRACT
A hemoglobin of high electrophoretic mobility was detected in a French male suffering from an acute leukemia; this hemoglobin was also present in his family. The variant was unstable and possessed an abnormal beta chain, in which a glycyl residue in position 64 (E8) was replaced by an aspartyl residue. This variant constitutes a new case of Hb J Calabria. Since the substituted E8 residue is in close spatial contact with that at B6, it was of interest to compare the properties of Hb J Calabria with those of other hemoglobins bearing substitutions at the same site.
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Base de dados:
MEDLINE
Assunto principal:
Hemoglobina J
/
Hemoglobinas Anormais
/
Leucemia
Limite:
Adult
/
Aged
/
Female
/
Humans
/
Male
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1977
Tipo de documento:
Article