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Biomedical subjects

J L Oudart

Publications and source records attributed to J L Oudart.

At least 19 recordsLinked to original sources
PubMed1977

Properties of the double substituted hemoglobin C Ziguinchor alpha2A beta 2 6 Glu replaced by Val 58 Pro replaced by Arg.

We have previously described the structural identification of the sickle hemoglobin variant Hb C Ziguinchor (alpha2A beta2 6 Glu replaced by Val, 58 Pro replaced by Arg). This hemoglobin was found in two generations (three members) of an African family. In two family members, the clinical picture resembled that typical of a sickle cell trait, while the third member showed a more extreme clinical condition due to complication by an iron deficiency anemia. The functional properties of Hb C Zig. in red blood cells or in dilute solutions were identical to those of Hb S. The gelling behaviour of deoxy Hb C Zig. was also indistinguishable from that of Hb S. These findings suggest that, in contrast to the case of Hb C Harlem, the second substitution in position beta58 in Hb C Zig. does not interfere with the intermolecular interactions determined by the sickle substitution.

Adult↗
PubMed1976

Hemoglobin Dakar = Hb Grady: demonstration by a new approach to the analysis of the tryptic core region of the alpha chain and oxygen equilibrium properties.

Preliminary studies have suggested that in Hb Dakar, histidine alpha112 was substituted by a glutamine. A re-investigation on this hemoglobin is presented in this report. A structural study has been performed using a new approach to analyse the tryptic core region of the human hemoglobin alpha chain. After tryptic digestion of the aminoethylated alpha chain, a secondary digestion of the tryptic core was carried out with chymotrypsin and with another protease, thermolysin. Analyses of the chymotryptic and thermolytic peptides indicated that the structure of Hb Dakar was identical to that of Hb Grady previously described by Huisman et al. who showed the insertion of three amino acid residues in position alpha115 or alpha118. The insertion, which was localized near two residues involved in the alpha1beta1 contact, did not produce a dissociation into dimers. Functional studies demonstrated a a slightly increased oxygen affinity, a lowered cooperativity and a normal Bohr effect. The low amount of the abnormal hemoglobin (8%) may in part be explained by a slight instability of the molecule.

Amino Acid Sequence↗