Ontology highlight
ABSTRACT:
SUBMITTER: Higashimoto Y
PROVIDER: S-EPMC2279806 | biostudies-literature | 2008 Mar
REPOSITORIES: biostudies-literature
Higashimoto Yuichiro Y Sugishima Masakazu M Sato Hideaki H Sakamoto Hiroshi H Fukuyama Keiichi K Palmer Graham G Noguchi Masato M
Biochemical and biophysical research communications 20080114 4
The lysine residues of rat heme oxygenase-1 (HO-1) were acetylated by acetic anhydride in the absence and presence of NADPH-cytochrome P450 reductase (CPR) or biliverdin reductase (BVR). Nine acetylated peptides were identified by MALDI-TOF mass spectrometry in the tryptic fragments obtained from HO-1 acetylated without the reductases (referred to as the fully acetylated HO-1). The presence of CPR prevented HO-1 from acetylation of lysine residues, Lys-149 and Lys-153, located in the F-helix. Th ...[more]