Chimeric β-galactosidase fusion proteins containing foreign peptides inserted either at the amino terminus or at inner sites have been studied regarding their purification properties. Whereas fusions at the amino terminal are retained less on TPEG-Sepharose columns than native β-galactosidase, the insertion in a specific site of the activating interface increases the binding of the modified β-galactosidase. This offers a way to construct more powerful β-galactosidase purification tags. © 1995 Chapman & Hall.
|Publication status||Published - 1 Oct 1995|