Purification of murine thymus leukemia antigen (TL). A quantitative assessment of limited proteolysis.

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.

• Authors: M Wolcott, T H Stanton, J L Williams, J C Bennett
• Journal: Biochemistry (Biochemistry) Vol. 14 Issue 22 Pg. 4792-6 (Nov 04 1975) ISSN: 0006-2960 [Print] United States
• PMID: 1182118 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Antigens
• Papain

Topics

• Animals
• Antigens (analysis)
• Cell Line
• Cell Survival
• Chromatography, DEAE-Cellulose
• Chromatography, Gel
• Leukemia, Experimental (immunology)
• Mice
• Molecular Weight
• Papain
• Thymus Gland (analysis, immunology)