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MALDI-target integrated platform for affinity-captured protein digestion

Ahmad-Tajudin A 1 , Adler B 2 , Ekström S 3 , Marko-Varga G 4 , Malm J 5 , Lilja H 6 Show all authors , Laurell T 7

Affiliations 

  • 1 Department of Measurement Technology and Industrial Electrical Engineering, Lund University, Box 118, 22100 Lund, Sweden; CREATE Health, Lund University, Medicon Village, Bldn 406, 22381 Lund, Sweden; Faculty of Biotechnology and Biomolecular Sciences, University Putra Malaysia, Serdang, Selangor 43400, Malaysia
  • 2 Department of Measurement Technology and Industrial Electrical Engineering, Lund University, Box 118, 22100 Lund, Sweden; CREATE Health, Lund University, Medicon Village, Bldn 406, 22381 Lund, Sweden. Electronic address: Belinda.Adler@elmat.lth.se
  • 3 Department of Measurement Technology and Industrial Electrical Engineering, Lund University, Box 118, 22100 Lund, Sweden; CREATE Health, Lund University, Medicon Village, Bldn 406, 22381 Lund, Sweden
  • 4 Department of Measurement Technology and Industrial Electrical Engineering, Lund University, Box 118, 22100 Lund, Sweden
  • 5 Department of Laboratory Medicine, Division of Clinical Chemistry, Lund University, Skåne University Hospital, 20502 Skåne, Sweden
  • 6 Department of Laboratory Medicine, Division of Clinical Chemistry, Lund University, Skåne University Hospital, 20502 Skåne, Sweden; Department of Laboratory Medicine, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA; Department of Surgery (Urology Service), Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA; Department of Medicine (GU Oncology Service), Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA; Nuffield Department of Surgical Sciences, University of Oxford, John Radcliffe Hospital, Oxford OX3 9DU, United Kingdom; Institute of Biomedical Technology, University of Tampere, Tampere 33520, Finland
  • 7 Department of Measurement Technology and Industrial Electrical Engineering, Lund University, Box 118, 22100 Lund, Sweden; CREATE Health, Lund University, Medicon Village, Bldn 406, 22381 Lund, Sweden; Department of Biomedical Engineering, Dongguk University, Seoul, Republic of Korea
Anal Chim Acta, 2014 Jan 7;807:1-8.
PMID: 24356215 DOI: 10.1016/j.aca.2013.08.051

Abstract

To address immunocapture of proteins in large cohorts of clinical samples high throughput sample processing is required. Here a method using the proteomic sample platform, ISET (integrated selective enrichment target) that integrates highly specific immunoaffinity capture of protein biomarker, digestion and sample cleanup with a direct interface to mass spectrometry is presented. The robustness of the on-ISET protein digestion protocol was validated by MALDI MS analysis of model proteins, ranging from 40 fmol to 1 pmol per nanovial. On-ISET digestion and MALDI MS/MS analysis of immunoaffinity captured disease-associated biomarker PSA (prostate specific antigen) from human seminal plasma are presented.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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