Abstract
AbstractSoybean leghemoglobin subcomponents were separated with good resolution in immobilized pH gradients, both at the analytical and preparative scales. In the latter case, the tedious step of gel washing could be omitted without affecting resolution. This procedure appeared as the only one suitable for preparing large amounts of highly purified leghemoglobin c1, c2 and c3, allowing their further characterization and an investigation of their specific roles in nitrogen fixation.
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