Pronase-based assay method for O6-methylguanine-DNA methyltransferase

Anal Biochem. 1996 May 1;236(2):284-9. doi: 10.1006/abio.1996.0168.

Abstract

A new, simple, and rapid assay method for O6-methylguanine-DNA methyltransferase (MGMT) has been developed. When [methyl-3H] DNA radiolabeled with N-[methyl-3H]-N-nitrosourea was incubated together with tissue homogenate, [methyl-3H] group was transferred to the enzyme, forming S-[methyl-3H]cysteine. In contrast to the previous methods which determined the amount of [methyl-3H] group removed from [methyl-3H] DNA, the present method measured the amount of [methyl-3H] transferred to the enzyme. This has been done by hydrolyzing the radiolabeled enzyme with pronase which is a proteolytic enzyme with a broad substrate specificity. On pronase digestion, [methyl-3H]-labeled enzyme becomes soluble in trichloroacetic acid. The method is very simple and rapid, and the only expensive equipment required is a scintillation counter which is a relatively routine piece of equipment at present. More than a dozen samples can be processed within 4-5 h without any difficulty. This new method has been employed in the studies on organ distribution of MGMT of rat and mouse.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cysteine / analogs & derivatives*
  • Cysteine / analysis
  • DNA Repair*
  • Hydrolysis
  • Methylation
  • Methyltransferases / analysis*
  • Mice
  • O(6)-Methylguanine-DNA Methyltransferase
  • Organ Specificity
  • Peptides / analysis*
  • Pronase
  • Rats
  • Time Factors
  • Tritium

Substances

  • Peptides
  • Tritium
  • S-methylcysteine
  • Methyltransferases
  • O(6)-Methylguanine-DNA Methyltransferase
  • Pronase
  • Cysteine