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Hb Marseille [α 2 β 2 N methionyl ‐ 2 (NA 2 ) His → Pro]: a new β chain variant having an extended N‐terminus
Author(s) -
Blouquit Y.,
Arous N.,
Lena D.,
Delanoe-Garin J.,
Lacombe C.,
Bardakdjian J.,
Vovan L.,
Orsini A.,
Rosa J.,
Galacteros F.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80624-9
Subject(s) - histidine , isoelectric focusing , chemistry , residue (chemistry) , hemoglobin , isoelectric point , chromatography , biochemistry , microbiology and biotechnology , enzyme , biology
A new abnormal hemoglobin was found in a diabetic Maltese woman by citrate agar electrophoresis. This variant was undetectable by isoelectric focusing. No hematological abnormalities were observed. The structural analysis included isolation of the abnormal β chain, high pressure liquid chromatography of the corresponding tryptic peptides and then microsequencing of the abnormal T 1 . These procedures revealed a double abnormality: the presence of a methionyl residue extending the NH 2 terminus and a histidine to proline substitution in position NA 2 .