Otro
Crystallization and X-ray diffraction data analysis of oxyhemoglobin-I from the catfish Liposarcus anisitsi (pisces)
Registro en:
Protein and Peptide Letters, v. 4, n. 5, p. 349-354, 1997.
0929-8665
2-s2.0-0001384330
Autor
Smarra, A. L S
Arni, R. K.
De Azevedo, W. F.
Colombo, M. F.
Bonilla-Rodriguez, G. O.
Resumen
Hemoglobin remains, despite the enormous amount of research involving this molecule, as a prototype for allosteric models and new conformations. Functional studies carried out on Hemoglobin-I from the South-American Catfish Liposarcus anisitsi [1] suggest the existence of conformational states beyond those already described for human hemoglobin, which could be confirmed crystallographically. The present work represents the initial steps towards that goal.