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pubmed-article:16099937pubmed:abstractTextAlbumin binds low-molecular-weight molecules, including proteins and peptides, which then acquire its longer half-life, thereby protecting the bound species from kidney clearance. We developed an experimental method to isolate albumin in its native state and to then identify [mass spectrometry (MS) sequencing] the corresponding bound low-molecular-weight molecules. We used this method to analyze pooled sera from a human disease study set (high-risk persons without cancer, n = 40; stage I ovarian cancer, n = 30; stage III ovarian cancer, n = 40) to demonstrate the feasibility of this approach as a discovery method.lld:pubmed
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pubmed-article:16099937pubmed:articleTitleAnalysis of albumin-associated peptides and proteins from ovarian cancer patients.lld:pubmed
pubmed-article:16099937pubmed:affiliationLaboratory of Pathology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.lld:pubmed
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