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PubMed1969

Subunit dissociation of certain abnormal human hemoglobins.

The extent of dissociation of various hemoglobins into subunits was estimated from their elution volumes (V(e)) on G-100 Sephadex. Under the same controlled conditions carboxyhemoglobins A, A3 (A(1)), F, S, and C all had the same elution volumes. The carboxy and cyanmet derivatives of hemoglobin Kansas (a variant with very low oxygen affinity) had a relatively high V(e), indicating a decreased mean molecular weight and therefore an increased tendency to form dimers and even monomers. Conversely, the liganded derivatives of hemoglobin Chesapeake (a variant with high oxygen affinity) had a relatively low V(e), suggestive of an impaired degree of subunit dissociation. Deoxyhemoglobin Chesapeake had a V(e) identical with that of deoxyhemoglobin A. Cat hemoglobin, known to have an unusually low oxygen affinity, was found to have a higher V(e) than human, dog, rabbit, rat, or guinea pig hemoglobins. Haptoglobin is thought to bind alphabeta dimers in preference to the alpha(2)beta(2)-tetramer. The comparative haptoglobin affinities of the human hemoglobins were measured by competition between the test hemoglobin and radioactive reference hemoglobin for haptoglobin binding sites. Hemoglobins A, F, S, and C all seemed to bind equally readily, but hemoglobin Kansas and cat hemoglobin showed a higher affinity, and hemoglobin Chesapeake a lower affinity. These results are in accord with recently proposed models which predict that hemoglobins which have an increased degree of subunit dissociation will have a low oxygen affinity, and vice versa.

Animals↗
PubMed1978

Hb J Camaguey alpha 2 141(HC3) Arg replaced by Gly beta 2: a new abnormal human hemoglobin.

An electrophoretic fast-moving hemoglobin was found in a Cuban family of Spanish descent. Structural studies demonstrated a replacement of arginine by glycine at alpha 141(HC3). This change is not associated with clinical symptoms, although the substitution is in one of the residues involved in the stabilization of the deoxy form of the hemoglobin molecule.

Amino Acids↗