Ontology highlight
ABSTRACT:
SUBMITTER: Distler AM
PROVIDER: S-EPMC1950290 | biostudies-literature | 2007 May
REPOSITORIES: biostudies-literature
Distler Anne M AM Kerner Janos J Hoppel Charles L CL
Biochimica et biophysica acta 20070328 5
The identification of post-translational modifications is difficult especially for hydrophobic membrane proteins. Here we present the identification of several types of protein modifications on membrane proteins isolated from mitochondrial outer membranes. We show, in vivo, that the mature rat liver mitochondrial carnitine palmitoyltransferase-I enzyme is N-terminally acetylated, phosphorylated on two threonine residues, and nitrated on two tyrosine residues. We show that long chain acyl-CoA syn ...[more]