Abstract

Differential screening-selected gene aberrative in neuroblastoma (DAN) encodes a protein which possesses metal binding motifs. Glutathione S-transferase DAN fusion protein had an ability to bind to Ni2+-immobilized affinity resin. Truncation of the C-terminal region including a (HX)n repeat of DAN caused a loss of binding ability to the affinity resin, suggesting that this region is essential for Ni2+-binding. DAN produced in cultured rat cells also had an affinity for Ni2+. Cross-linking experiments demonstrated that the C-terminal region might function as a protein-protein interacting domain.

Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call