In:
IUBMB Life, Wiley, Vol. 63, No. 5 ( 2011-05), p. 323-328
Abstract:
The extracellular hemoglobin multimer of the planorbid snail Biomphalaria glabrata , intermediate host of the human parasite Schistosoma mansoni , is presumed to be a 1.44 MDa complex of six 240 kDa polypeptide subunits, arranged as three disulfide‐bridged dimers. The complete amino acid sequence of two subunit types (BgHb1 and BgHb2), and the partial sequence of a third type (BgHb3) are known. Each subunit encompasses 13 paralogus heme domains, and N‐terminally a smaller plug domain responsible for subunit dimerization. We report here the recombinant expression of different functional fragments of BgHb2 in Escherichia coli , and of the complete functional subunits BgHb1 and BgHb2 in insect cells; BgHb1 was also expressed as disulfide‐bridged dimer (480 kDa). Oxygen‐binding measurements of the recombinant products show a P 50 of about 7 mmHg and the absence of a significant cooperativity or Bohr effect. The covalently linked dimer of BgHb1, but not the monomer, is capable to form aggregates closely resembling native BgHb molecules in the electron microscope. © 2011 IUBMB IUBMB Life, 63(5): 323–328, 2011
Type of Medium:
Online Resource
ISSN:
1521-6543
,
1521-6551
Language:
English
Publisher:
Wiley
Publication Date:
2011
detail.hit.zdb_id:
2009952-6
detail.hit.zdb_id:
2485214-4
SSG:
12
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