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Rat liver polysome N alpha-acetyltransferase: isolation and characterization.

R Yamada1, R A Bradshaw

  • 1Department of Biological Chemistry, College of Medicine, University of California, Irvine 92717.

Biochemistry
|January 29, 1991
PubMed
Summary

Rat liver polysome N alpha-acetyltransferase was purified to homogeneity. This enzyme, crucial for protein modification, exhibits characteristics similar to yeast enzymes but differs from avian counterparts.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • N alpha-acetyltransferase (NAT) enzymes play a vital role in post-translational modification of proteins.
  • Understanding the properties of NAT from different species can provide insights into conserved and divergent enzymatic mechanisms.

Purpose of the Study:

  • To purify and characterize rat liver polysome N alpha-acetyltransferase (NAT).
  • To compare the biochemical properties of rat liver NAT with those of NAT from other species, such as yeast and hen oviduct.

Main Methods:

  • Purification of the enzyme to homogeneity using a four-step procedure: ammonium sulfate precipitation, gel filtration, hydroxylapatite chromatography, and Mono Q ion exchange chromatography.
  • Enzyme stabilization using EDTA and deoxycholate.

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  • Determination of native and subunit molecular weights, pH optimum, and sensitivity to various inhibitors.

    • Main Results:

    • The purified rat liver NAT has a native molecular weight of 190,000 Da and a subunit molecular weight of 95,000 Da, indicating a homodimeric structure.
    • The enzyme exhibits a pH optimum of 8.0.
    • Strong inhibition was observed with Cl-, I-, SCN-, and ClO4-, with lesser inhibition by sulfate and acetate. Ammonium ion showed partial inhibition, while phosphate, citrate, F-, Na+, and K+ had no effect. The enzyme is also sensitive to iodoacetic acid.

    Conclusions:

    • Rat liver polysome NAT has been successfully purified and characterized.
    • The enzyme's properties suggest it is more similar to yeast N alpha-acetyltransferase than to the hen oviduct enzyme, despite differences in amino acid composition.
    • The findings contribute to the understanding of NAT diversity and function across species.