Influence of mercaptoethanol on the isolation of mercury-binding proteins from the gills of Mytilus edulis

1. 1. Use of the reducing agent 2-mercaptoethanol during extraction and isolation of low mol. wt, mercury-binding proteins of mussel gills resulted in an appearance of significant quantities of mercury associated with substances of <3000 daltons. 2. 2. The source of this mercury was mercury originally bound to the pellet, high mol. wt proteins, and low mol. wt, mercury-binding proteins. 3. 3. This shift in mercury distribution is regarded as a procedural artifact caused by reduction of mercury-binding sites and possible association of released mercury with mercaptoethanol. 4. 4. Use of mercaptoethanol did not release significant amounts of the metal-binding proteins from the high mol. wt protein pool.