Abstract：
:Isolated alpha and beta chains from Xenopus laevis hemoglobin have been purified. The isolation procedure yields native alpha chains whose functional behavior has been characterized and compared with that of human alpha chains. Isolated beta chains in the presence of oxygen are characterized by low stability, and hence their functional characterization was limited to the CO binding kinetics. When stoichiometric amounts of the isolated alpha and beta chains are mixed, a tetramer characterized by heme-heme interactions and oxygen affinity comparable to that of the native molecule is readily reconstituted. Moreover, both chains, under appropriate conditions, form stable hybrid tetramers with the partner subunits from human hemoglobin; results on the functional properties of these hybrid hemoglobins are presented and discussed in relation to the stereochemical model of the Root effect.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Condò SG,Giardina B,Bellelli A,Brunori Mdoi
10.1021/bi00395a022subject
Has Abstractpub_date
1987-10-20 00:00:00pages
6718-22issue
21eissn
0006-2960issn
1520-4995journal_volume
26pub_type
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