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Chiroptical and physicochemical properties of the extracellular haemoglobin from Cirriformia tentaculata
Journal article

Chiroptical and physicochemical properties of the extracellular haemoglobin from Cirriformia tentaculata

Thomas J. Difeo, Anthony W. Addison and Thomas F. Kumosinski
Comparative biochemistry and physiology. B, Comparative biochemistry, v 97(2), pp 391-399
1990
DOI: https://doi.org/10.1016/0305-0491(90)90297-7
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Abstract

Master of Music (MM) DTE Mb Hb m g PPIX Hb EDTA
1. 1. The extracellular respiratory protein from the vascular system of the poylychaete annelid Cirriformia tentaculata is a giant haemoglobin with a minimum molecular mass subunit of 16.5±0.5 kDa . 2. 2. λ max Values and the respective molar extinction coefficients for selected ligand-bound states are reported. 3. 3. Nitrosyl autoreduction kinetics and the azide binding affinity are examined. 4. 4. Circular dichroism spectra show a helix content similar to that of human haemoglobin. 5. 5. Using previously characterized proteins from the literature as models, an experimental approach is developed to quantitatively estimate the haem orientation of proteins from circular dichroism measurements. 6. 6. The majority haem orientation in Cirriformia tentaculata haemoglobin is identical with that of human haemoglobin.

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Collaboration types
Domestic collaboration
Web of Science research areas
Biochemistry & Molecular Biology
Zoology
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