DNA ligase from mouse Ehrlich ascites tumor cells.

Abstract

The molecular (Mr = 120,000; s20, w = 5S) and catalytic properties (Km (ATP) = 3 microM; Km (nicked DNA) = 0.2 microM; Km (Mg2+) = 3 mM) of DNA ligase from mouse Ehrlich ascites tumor cells are similar to those of the enzymes from calf thymus and rodent liver. The activity level of DNA ligase from the tumor cells is about 10-fold higher than that from mouse liver. Immunochemical titration of DNA ligase with antibodies against the calf thymus enzyme showed that the higher level of DNA ligase activity in the tumor cells is due to an increase in enzyme quantity and not to elevation of the catalytic efficiency of the enzyme molecule. These results suggest that there is little apparent difference between the qualities of DNA ligases from the tumor cells and normal tissues of rodents and calf.

• Authors: H Teraoka, M Sawai, K Tsukada
• Journal: Journal of biochemistry (J Biochem) Vol. 95 Issue 5 Pg. 1529-32 (May 1984) ISSN: 0021-924X [Print] England
• PMID: 6746618 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Antigen-Antibody Complex
• Immune Sera
• Adenosine Monophosphate
• Adenosine Triphosphate
• DNA Ligases
• Polynucleotide Ligases

Topics

• Adenosine Monophosphate (metabolism)
• Adenosine Triphosphate (metabolism)
• Animals
• Antigen-Antibody Complex
• Carcinoma, Ehrlich Tumor (enzymology)
• DNA Ligases (isolation & purification, metabolism)
• Immune Sera
• Kinetics
• Mice
• Molecular Weight
• Polynucleotide Ligases (isolation & purification)
• Protein Binding