The kinetic and molecular weight characteristics of the non-inducible rat liver and the inducible rat pineal gland N-acetyltransferases were determined and compared. Both enzymes exhibited initial rate kinetics suggestive of a ping-pong mechanism implying the existence of an acetylated enzyme intermediate. The elution characteristics of the enzyme activities on Sephadex G-100 indicate an apparent molecular weight for the liver enzyme of 26,000 while the pineal gland N-acetyltransferase eluted at an apparent weight of 39,000. Molecular weight determinations performed in the presence of β-mercaptoethylamine suggest active subunit molecular weights of 10,000 - 12,000 daltons for the pineal gland and liver enzymes, respectively.
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jul 11 1977|