التفاصيل البيبلوغرافية
| العنوان: |
Recombinant functional multidomain hemoglobin from the gastropod Biomphalaria glabrata |
| المؤلفون: |
Jürgen Markl, Sabrina Keller, Bernhard Lieb, Nadja Hellmann, Ralf Dürr, V. Moeller, Arne Moeller, Ladan Sarraf-Zadeh, Stefanie Heinz |
| المصدر: |
Moeller, V, Dürr, R, Sarraf-Zadeh, L, Keller, S, Heinz, S, Hellmann, N, Möller, A, Lieb, B & Markl, J 2011, ' Recombinant functional multidomain hemoglobin from the gastropod Biomphalaria glabrata ', IUBMB Life, vol. 63, no. 5, pp. 323-8 . https://doi.org/10.1002/iub.453Test |
| بيانات النشر: |
Wiley, 2011. |
| سنة النشر: |
2011 |
| مصطلحات موضوعية: |
Protein subunit, Clinical Biochemistry, Cooperativity, medicine.disease_cause, Biochemistry, law.invention, Hemoglobins, chemistry.chemical_compound, law, Genetics, medicine, Animals, Humans, Biomphalaria glabrata, Protein Structure, Quaternary, Molecular Biology, Escherichia coli, Peptide sequence, Heme, Biomphalaria, biology, Schistosoma mansoni, Cell Biology, biology.organism_classification, Recombinant Proteins, Oxygen, Protein Subunits, chemistry, Recombinant DNA, Oxygen binding |
| الوصف: |
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 P50 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 |
| تدمد: |
1521-6543 |
| الوصول الحر: |
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8911e72e9a5dc3053220edcaee1b5467Test
https://doi.org/10.1002/iub.453Test |
| حقوق: |
OPEN |
| رقم الانضمام: |
edsair.doi.dedup.....8911e72e9a5dc3053220edcaee1b5467 |
| قاعدة البيانات: |
OpenAIRE |
