Characterization of hemoglobin from Phoronis architecta (phoronida) |
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| Institution: | 1. Department of Biotechnology, Noida Institute of Engineering & Technology (NIET), Greater Noida, India;2. Department of Pharmaceutical Sciences and Technology, Birla Institute of Technology, Mesra, Ranchi, India;1. Department of Economics and Management, University of Brescia, 74/B Brescia, Italy;2. Scuola Normale Superiore di Pisa, Piazza del Cavalieri, 7–56126 Pisa, Italy;3. Department of Statistics, University Carlos III de Madrid, Avda. de la Universidad 30, 28911-Leganés, Spain;4. UC3M-BS Institute for Financial Big Data (FiBiD), Universidad Carlos III de Madrid, 28903, Getafe, Madrid, Spain |
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| Abstract: | - 1.1. Phoronis architecta hemoglobin is composed of four distinct hemoglobin subunits with minimum MW's of 16–17,000 or 17–19,000 daltons. All four hemoglobins are monomeric when oxygenated. Two of the monomers combine to form dimers when bound with carbon monoxide.
- 2.2. In cellulo, Phoronis architecta hemoglobin has a half-saturation (P50) value of 1.3 ± 0.1 mm Hg, shows cooperative oxygen binding (Hill coefficient = 2.7 ± 0.3), and no Bohr effect from pH 6.6 to 7.9. In vitro, the hemoglobin has a P50 of 0.76 ± 0.21 mm Hg but shows no cooperativity (0.90 ± 0.15 (SD)).
- 3.3. The oxygen dissociation constant (Koff) from hemoglobin is 2.7 ± 0.2 sec?1, and the computed oxygen association constant (Kon) is 2.5 × 106 M?1 · sec?1 (1.9–3.6 × 106 M?1 · sec?1).
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