دورية أكاديمية
A method for the selective isolation and enrichment of carrier protein-bound low-molecular weight proteins and peptides in the blood.
| العنوان: | A method for the selective isolation and enrichment of carrier protein-bound low-molecular weight proteins and peptides in the blood. |
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| المؤلفون: | Camerini S; Center for Applied Proteomics and Molecular Medicine, George Mason University, Manassas, VA, USA; Istituto Superiore di Sanità, Rome, Italy., Polci ML, Liotta LA, Petricoin EF, Zhou W |
| المصدر: | Proteomics. Clinical applications [Proteomics Clin Appl] 2007 Feb; Vol. 1 (2), pp. 176-84. Date of Electronic Publication: 2007 Jan 22. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Wiley-VCH Country of Publication: Germany NLM ID: 101298608 Publication Model: Print-Electronic Cited Medium: Print ISSN: 1862-8346 (Print) Linking ISSN: 18628346 NLM ISO Abbreviation: Proteomics Clin Appl Subsets: PubMed not MEDLINE |
| أسماء مطبوعة: | Original Publication: Weinheim : Wiley-VCH, c2007- |
| مستخلص: | The low molecular weight (LMW) region of the circulatory proteome, thought to contain a rich source of biomarkers, resides in vivo, in a complexed state with larger, highly abundant resident proteins. Consequently, serum fractionation approaches that deplete the high-abundance proteins under native conditions will remove much of the LMW proteome. We describe a new strategy to systematically collect, isolate and enrich the LMW molecules that would be otherwise eliminated during the depletion of high-abundance circulatory proteins based on continuous elution electrophoresis. We employ strong denaturing conditions to disrupt association with the high-abundance carrier proteins followed by fractionation and removal of SDS. Under denaturation, the LMW molecules were effectively stripped from the highly abundant carrier proteins. We then removed the SDS by ion exchange matrix sequestration and concentrated the fractions. The outcome is a series of SDS-free fractions of LMW molecules. The isolated fractions were then analyzed by enzymatic digestion followed by LC-MS/MS analysis. The yield of multiple peptide hits as well as the total number of identifications significantly increased (50%) compared to unfractionated serum. The method yielded a 30% higher number of low-abundance serum proteins compared to direct sequencing of unfractionated serum. (Copyright © 2007 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.) |
| تواريخ الأحداث: | Date Created: 20101208 Date Completed: 20121002 Latest Revision: 20101207 |
| رمز التحديث: | 20240628 |
| DOI: | 10.1002/prca.200600618 |
| PMID: | 21136667 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1862-8346 |
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| DOI: | 10.1002/prca.200600618 |