Initial biophysical characterization of Amynthas gracilis giant extracellular hemoglobin (HbAg)
Author:
Funder
FAPESP
Publisher
Springer Science and Business Media LLC
Subject
General Medicine,Biophysics
Link
https://link.springer.com/content/pdf/10.1007/s00249-020-01455-8.pdf
Reference31 articles.
1. Bachega JFR, Maluf FV, Andi B, Pereira HD, Carazzollea MF, Orville AM, Tabak M, Brandao-Neto J, Garratt RC, Reboredo EH (2015) The structure of the giant haemoglobin from Glossoscolex paulistus. Acta Crystallogr Sect D Struct Biol 71:1257–1271. https://doi.org/10.1107/S1399004715005453
2. Bradford MM (1976) A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254. https://doi.org/10.1006/abio.1976.9999
3. Carvalho FAO, Carvalho JWP, Santiago PS, Tabak M (2011a) Further characterization of the subunits of the giant extracellular hemoglobin of Glossoscolex paulistus (HbGp) by SDS–PAGE electrophoresis and MALDI-TOF–MS. Process Biochem 46:2144–2151. https://doi.org/10.1016/j.procbio.2011.08.013
4. Carvalho FAO, Santiago PS, Borges JC, Tabak M (2011b) Molecular masses and sedimentation coefficients of extracellular hemoglobin of Glossoscolex paulistus: alkaline oligomeric dissociation. Int J Biol Macromol 48:183–193. https://doi.org/10.1016/j.ijbiomac.2010.11.002
5. Carvalho FAO, Carvalho JWP, Alves FR, Tabak M (2013a) PH effect upon HbGp oligomeric stability: characterization of the dissociated species by AUC and DLS studies. Int J Biol Macromol 59:333–341. https://doi.org/10.1016/j.ijbiomac.2013.04.070
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