In vitro oxidative footprinting provides insight into apolipoprotein B-100 structure in low-density lipoprotein.

ABSTRACT: Low-density lipoprotein (LDL) is a major cholesterol carrier in human blood. Oxidations of apolipoprotein B-100 (apo B-100, LDL protein) could be proatherogenic and play critical roles in early stages of plaque formation in the arterial wall. The structure of apo B-100 is still poorly understood, partially due to its size (550 KDa, 4563 amino acids). To gain an insight into LDL structure, we mapped the regions of apo B-100 in human LDL that were prone to oxidation using peroxynitrite and hypochlorite as probes. In this study, LDL was incubated with various concentrations of peroxynitrite and sodium hypochlorite in bicarbonate buffer. The LDL protein apo B-100 was delipidated, denatured, alkylated, and subjected to tryptic digestion. Tryptic peptides were analyzed employing LC-MS/MS. Databa

SUBMITTER: Chakraborty S 

PROVIDER: S-EPMC4320993 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature