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Titolo:
Analysis of native proteins from biological fluids by biomolecular interaction analysis mass spectrometry (BIA/MS): exploring the limit of detection,identification of non-specific binding and detection of multi-protein complexes
Autore:
Nedelkov, D; Nelson, RW;
Indirizzi:
Intrins Bioprobes Inc, Tempe, AZ 85281 USA Intrins Bioprobes Inc Tempe AZUSA 85281 oprobes Inc, Tempe, AZ 85281 USA
Titolo Testata:
BIOSENSORS & BIOELECTRONICS
fascicolo: 9-12, volume: 16, anno: 2001,
pagine: 1071 - 1078
SICI:
0956-5663(200112)16:9-12<1071:AONPFB>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
CLARA CELL PROTEIN; PLASMON RESONANCE SENSORS; RENAL-FUNCTION; MALDI-MS; SURFACE; SERUM; BIOSENSORS; MARKER; TOXINS; CC16;
Keywords:
BIA/MS; SPR; MALDI-TOF mass spectrometry; limit of detection; protein complexes; non-specific binding;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Nelson, RW Intrins Bioprobes Inc, 625 S Smith Rd,Suite 22, Tempe, AZ 85281USA Intrins Bioprobes Inc 625 S Smith Rd,Suite 22 Tempe AZ USA 85281
Citazione:
D. Nedelkov e R.W. Nelson, "Analysis of native proteins from biological fluids by biomolecular interaction analysis mass spectrometry (BIA/MS): exploring the limit of detection,identification of non-specific binding and detection of multi-protein complexes", BIOSENS BIO, 16(9-12), 2001, pp. 1071-1078

Abstract

Biomolecular interaction analysis mass spectrometry (BIA/MS) is a two-dimensional analytical technique that quantitatively and qualitatively detects analytes of interests. In the first dimension, surface plasmon resonance (SPR) is utilized for detection of biomolecules in their native environment. Because SPR detection is non-destructive, analyte(s) retained on the SPR-active sensor surface can be analyzed in a second dimension using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry. The qualitative nature of the MALDI-TOF MS analysis complements the quantitative character of SPR sensing and overcomes the shortcomings of the SPR detection stemming from the inability to differentiate and characterize multi-protein complexes and non-specific binding. In this work, the benefit of performing NIS analysis following SPR sensing is established. Retrieval and detection of four markers present in biological fluids (cystatin C, beta-2-microglobulin, urinary protein 1 and retinol binding protein) was explored to demonstrate the effectiveness of BIA/MS in simultaneous detection ofclinically related biomarkers and delineation of non-specific binding. Furthermore, the BIA/MS limit of detection at very low SPR responses was investigated. Finally, detection of in-vivo assembled protein complexes was achieved for the first time using BIA/MS. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 02:49:22