Analysis of Albumin-Associated Peptides and Proteins from Ovarian Cancer Patients | Zendy

Mark S. Lowenthal | Zendy; Arpita Mehta | Zendy; Kristina Frogale | Zendy; Russell Bandle | Zendy; Robyn P. Araujo | Zendy; Brian L. Hood | Zendy; Timothy D. Veenstra | Zendy; Thomas P. Conrads | Zendy; Paul K. Goldsmith | Zendy; David A. Fishman | Zendy; Emanuel F. Petricoin | Zendy; Lance A. Liotta | Zendy

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Analysis of Albumin-Associated Peptides and Proteins from Ovarian Cancer Patients

Author(s) -

Mark S. Lowenthal,

Arpita Mehta,

Kristina Frogale,

Russell Bandle,

Robyn P. Araujo,

Brian L. Hood,

Timothy D. Veenstra,

Thomas P. Conrads,

Paul K. Goldsmith,

David A. Fishman,

Emanuel F. Petricoin,

Lance A. Liotta

Publication year - 2005

Publication title -

clinical chemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.705

H-Index - 218

eISSN - 1530-8561

pISSN - 0009-9147

DOI - 10.1373/clinchem.2005.052944

Subject(s) - albumin , blot , peptide , gel electrophoresis , biology , ovarian cancer , serum albumin , chemistry , biochemistry , proteome , human serum albumin , in vivo , microbiology and biotechnology , cancer , genetics , gene

Albumin 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.

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