Probable identity of the β chains from the two chicken hemoglobin components

Reduction in potency and reversal of left‐shifting activity of BW12C with the major and minor components of chicken hemoglobin

“…The sequences of the&chains of both forms of chicken hemoglobin are apparently identical [17,18], and the difference between the effects of BW12C on the major and minor components must therefore depend on their different a-chain sequences. The most obvious difference in the (Ychain terminal amino region is the replacement Val lcu+Met, and this would be expected to disfavor binding at this locus since model studies of the Schiff base formation of pyridoxal and amino 132 acids [19] showed an approx.…”

“…The right-shifted curves with chicken minor hemoglobin suggest that binding at the &terminus in the deoxy conformation is now the dominant binding mode, and reaction at this site is supported by the competition for binding with inositol hexaphosphate. The sequences of the&chains of both forms of chicken hemoglobin are apparently identical [17,18], and the difference between the effects of BW12C on the major and minor components must therefore depend on their different a-chain sequences. The most obvious difference in the (Ychain terminal amino region is the replacement Val lcu+Met, and this would be expected to disfavor binding at this locus since model studies of the Schiff base formation of pyridoxal and amino 132 acids [19] showed an approx.…”