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Biomedical subjects

S Charache

Publications and source records attributed to S Charache.

At least 127 records · Page 7Linked to original sources
PubMed1972

Hemoglobin Malmö Beta-97 (FG-4) histidine--glutamine: a cause of polycythemia.

A striking history of familial polycythemia led to a search for an abnormal hemoglobin. None could be demonstrated by routine electrophoretic methods, but the propositus' hemolysate had increased oxygen affinity. Manipulation of the conditions of electrophoresis, and chromatographic methods, permitted identification of hemoglobin Malmö. Studies of hemolysates demonstrated a normal Bohr effect, decreased heme-heme interaction (n=1.58), and a p50 of 1.3 mm Hg at 10 degrees C and pH 7.2. The amino acid substitution occurs in the same position (FG-4) as that of hemoglobin Chesapeake, but in the beta-chain rather than the alpha-chain. The two types of hemolysate have different pathophysiologic properties, and carriers of hemoglobin Malmö exhibit more striking hematologic abnormalities.

Amino Acid Sequence↗
PubMed1971

Oxygen equilibrium of hemoglobin J Cape Town.

Polycythemia in carriers of hemoglobin J Cape Town or hemoglobin Chesapeake is thought to be produced by increased oxygen affinity of their blood. Both hemoglobins involve substitution of amino acid residue alpha FG-4. Measurements reported here, of the oxygen equilibrium of purified hemoglobin J Cape Town, permit direct comparison of the two hemoglobins. J Cape Town exhibits lower oxygen affinity, and greater heme-heme interaction, than Chesapeake; both exhibit normal Bohr effects. Substitution of one polar amino acid residue for another of opposite charge (arginine --> glutamic acid) thus appears to create less disruption of the interface between alpha- and beta-chains than substitution of a nonpolar residue (arginine --> leucine).

Amino Acid Sequence↗