Population studies of intact vitamin D binding protein by affinity capture ESI-TOF-MS.
Blood plasma proteins with molecular weights greater than approximately 30 kDa are refractory to comprehensive, high-throughput qualitative characterization of microheterogeneity across human populations. Analytical techniques for obtaining high mass resolution for targeted, intact protein characterization and, separately, high sample throughput exist, but efficient means of coupling these assay characteristics remain rather limited. This article discusses the impetus for analyzing intact proteins in a targeted manner across populations and describes the methodology required to couple mass spectrometric immunoassay with electrospray ionization mass spectrometry for the purpose of qualitatively characterizing a prototypical large plasma protein, vitamin D binding protein, across populations.
Borges
Chad R
CR
Molecular Biosignatures Analysis Unit, The Biodesign Institute at Arizona State University, Tempe, AZ 85287, USA. chad.borges@asu.edu
Jarvis
Jason W
JW
Oran
Paul E
PE
Rogers
Stephen P
SP
Nelson
Randall W
RW
D000483:Alleles; D015415:Biomarkers / Q000097:blood; D001709:Biotechnology; D001774:Blood Chemical Analysis / Q000379:methods; D002853:Chromatography, Liquid / Q000379:methods; D005828:Genetics, Population; D005838:Genotype; D006031:Glycosylation; D006801:Humans; D007118:Immunoassay / Q000379:methods; D040901:Proteomics / Q000379:methods; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*; D014809:Vitamin D-Binding Protein / Q000097:blood* / Q000737:chemistry / Q000235:genetics
D015415:Biomarkers; D014809:Vitamin D-Binding Protein