Purification of Murine Thymus Leukemia Antigen (TL). A Quantitative Assessment of Limited Proteolysis

Academic Article

Abstract

  • The murine thymus leukemia antigen (TL) has been solubilized from the tumor ASL1 and from an established cell line ASL1W, by papain digestion. When a 15-min digest was chromatographed on Sephadex G-200, two peaks of TL activity were eluted with apparent molecular weights of approximately 58,000 and 31,000. Chromatography of a 30-min digest under the same conditions resulted in elution of a single peak of activity with an apparent molecular weight of 58,000. Additional purification was carried out on the 58,000 molecular weight material by absorption to, and elution from DEAE-cellulose. The combination of gel filtration and ion exchange chromatography resulted in approximately a 150-fold purification. © 1975, American Chemical Society. All rights reserved.
  • Authors

    Published In

  • Biochemistry  Journal
  • Digital Object Identifier (doi)

    Author List

  • Wolcott M; Stanton TH; Williams JL; Bennett JC
  • Start Page

  • 4792
  • End Page

  • 4796
  • Volume

  • 14
  • Issue

  • 22