Effects of buffer composition, pH and temperature on oxygen binding by planorbid snail haemoglobins

Aardt, W.J. van; Naude, K.

doi:10.1080/02541858.1990.11448183

Cited by 6 publications

(1 citation statement)

References 20 publications

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“…These characters may be adaptive in favoring O 2 loading as pH increases at respiratory surfaces (5,26). Similar Bohr effects have been recorded for the hemoglobins of two other planorbids, Planorbarius corneus and Heliosoma trivolis (27,28).…”

Section: Oxygen-binding Properties Of Recombinant Bghbmentioning

confidence: 48%

Recombinant functional multidomain hemoglobin from the gastropod Biomphalaria glabrata

et al. 2011

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SummaryThe 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 disulfidebridged 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.

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Section: Oxygen-binding Properties Of Recombinant Bghbmentioning

confidence: 48%