Mass spectrometric measurements of the apolipoproteins of bovine ( Bos taurus) HDL

• Published in: Comparative biochemistry and physiology. Part D, Genomics & proteomics Genomics & proteomics, 2012-03, Vol.7 (1), p.9-13
• Main Authors: Della Donna, Lorenza, Bassilian, Sara, Souda, Puneet, Nebbia, Carlo, Whitelegge, Julian P., Puppione, Donald L.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; apoC-I; apoHDL; Apolipoprotein A-I - chemistry; Apolipoprotein A-I - metabolism; Apolipoprotein C-III - chemistry; Apolipoprotein C-III - metabolism; Apolipoproteins - chemistry; Apolipoproteins - metabolism; Apolipoproteins A - chemistry; Apolipoproteins A - metabolism; Cattle - metabolism; Cholesteryl ester transfer protein; Lipoproteins, HDL - chemistry; Lipoproteins, HDL - metabolism; Mass spectrometry; Molecular Sequence Data; Spectrometry, Mass, Electrospray Ionization
• ISSN: 1744-117X; 1878-0407
• DOI: 10.1016/j.cbd.2011.10.001

As is the case in most mammals, high density lipoproteins (HDL) also comprise the major group of lipid carriers that circulate in bovine ( Bos taurus) blood. As a continuation of our proteogenomic studies of mammalian apolipoproteins, we have obtained molecular masses for several of the apolipoproteins associated with bovine HDL. The major apolipoprotein on the HDL surface is apoA-I, but other apolipoproteins were also detected. Using electrospray-ionization mass spectrometry (ESI-MS), we report on values for apolipoproteins, A-I, proA-I and A-II, as well as post-translationally modified apoA-I. Analyses of tryptic fragments did reveal the presence of apoA-IV and apoC-III. However, in contrast to our previous studies of other mammalian HDL, we did not detect apoC-I. Interestingly, examination of the current assembly for the bovine genome does not show any evidence for an apoC-I gene.