Two enzymes concerned in peptide hormone α-amidation are synthesized from a single mRNA

This publication has 19 references indexed in Scilit:

• A novel enzyme from bovine neurointermediate pituitary catalyzes dealkylation of .alpha.-hydroxyglycine derivatives, thereby functioning sequentially with peptidylglycine .alpha.-amidating monooxygenase in peptide amidation
  Biochemistry, 1990
• Peptidylglycine α-amidating reaction: Evidence for a two-step mechanism involving a stable intermediate at neutral pH
  Biochemical and Biophysical Research Communications, 1990
• Enzymatic peptidyl .alpha.-amidation proceeds through formation of an .alpha.-hydroxyglycine intermediate
  Journal of the American Chemical Society, 1989
• Biosynthesis of the C-terminal amide in peptide hormones
  Bioscience Reports, 1987
• High-efficiency transformation of mammalian cells by plasmid DNA.
  Molecular and Cellular Biology, 1987
• Human preprovasoactive intestinal polypeptide contains a novel PHI-27-like peptide, PHM-27
  Nature, 1983
• A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
  Analytical Biochemistry, 1983
• Deduced amino acid sequence from the bovine oxytocin–neurophysin I precursor cDNA
  Nature, 1983
• Mechanism of C-terminal amide formation by pituitary enzymes
  Nature, 1982
• Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
  Biochemistry, 1979