The α-globin of human hemoglobin was expressed in Escherichia coli and was refolded with
heme in the presence and in the absence of native β-chains. The functional and structural …

Individual, soluble human α-globin chains were expressed in bacteria with exogenous heme
and methionine aminopeptidase. The yields of soluble α chains in bacteria were …

Analysis of the conformational differences between the oxy and deoxy forms of hemoglobin
is complicated by shifting coordinate systems and correlated motions between different parts …

The N-terminal 18-amino acid sequence of the β-chain of hemoglobin, as far as the end of
the A helix, has been replaced by the corresponding sequence of the γ-chain of fetal …

Human hemoglobin produced in the Escherichia coli coexpression system of Hernan et
al.[(1992) Biochemistry 31, 8619− 8628] has been transformed into a functionally …

Rates of in vitro synthesis of radiolabeled γ and β chains made in a cell-free transcription/
translation system were similar, but expressed globin chains were unstable. The addition of …

In our previous work, we demonstrated that the replacement of the" heme binding module," a
segment from F1 to G5 site, in myoglobin with that of hemoglobin α-subunit converted the …

Three variants of tetrameric human hemoglobin, with changes at the α 1 β 2/α 2 β 1-
interface, at the α 1 β 1/α 2 β 2-interface, and at both interfaces, have been constructed. At α …

Structural and functional investigations of recombinant human hemoglobin A (HbA) isolated
from the erythrocytes of transgenic swine coexpressing human alpha-and beta-globins have …

Recombinant α 2 β 2 tetrameric Hb expressed and assembled in Escherichia coli has been
characterized extensively. Electrospray mass spectrometry and optical and electron …