Crystallographic studies of fish hemoglobins

Abstract

The present work reports our succesfull experience concerning crystallization of four fish hemoglobins from three Brazilian species of Teleosts: Liposarcus anisitsi, Brycon cephalus and Piaractus mesopotamicus. The data shown here is part of a systematic functional and structural study of fish hemoglobins with the aim of better understanding the outstanding range of functional and structural properties exhibited by these proteins. We also present a reduced sparse-matrix method for crystallization of fish hemoglobins, which can reduce the amount of hemoglobin initially used in the crystallization experiments.

The crystal structure of haemoglobin from Atlantic cod

“…A new purification protocol was established by modifying the method described previously by Delatorre et al (2000). The sample was loaded onto an anion-exchange chromatography column at high pH and was eluted by a gradual reduction of the pH.…”

Crystallization, preliminary X-ray analysis and molecular-replacement solution of haemoglobin-II from the fish matrinxã (Brycon cephalus)

“…Usually, protons bind to haemoglobin (Hb) when the protein downloads oxygen at the tissue level (the Haldane effect) and they simultaneously produce a decrease in oxygen af®nity (the alkaline Bohr effect) (Fago et al, 1999;Seixas et al, 1999;Delatorre et al, 2000Delatorre et al, , 2001.…”