[10] High-performance liquid affinity chromatography

Larsson, Per‐Olof

doi:10.1016/s0076-6879(84)04091-x

Cited by 149 publications

(98 citation statements)

References 6 publications

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“…The diol coverage of the support, 2.98 0.20 mmole/m 2 , as determined in triplicate by the periodate oxidation method [23,24], was comparable to the expected value of about 2.5 mmole/m 2 for a well-coated support [25]. The diol groups were oxidized with periodic acid [25] …”

Section: Immunoaffinity Supportsupporting

confidence: 53%

Selective trace enrichment by immunoaffinity capillary electrochromatography on-line with capillary zone electrophoresis — laser-induced fluorescence

et al. 1999

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Section: Immunoaffinity Supportsupporting

confidence: 53%

Selective trace enrichment by immunoaffinity capillary electrochromatography on-line with capillary zone electrophoresis — laser-induced fluorescence

et al. 1999

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“…After purification and activation [17], silica gel was subjected to surface modification with glycidoxypropyltrimethoxysilane (GLYMO) in dry toluene in the presence of triethylamine (Figure 1b) [18].…”

Section: Particle Preparation and Derivatizationmentioning

confidence: 99%

Material-enhanced laser desorption/ionization (MELDI)—A new protein profiling tool utilizing specific carrier materials for time of flight mass spectrometric analysis

Feuerstein

Najam‐ul‐Haq

Rainer

et al. 2006

J. Am. Soc. Mass Spectrom.

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Over the past couple of years, proteomics pattern analysis has emerged as an effective method for the early diagnosis of diseases such as ovarian, breast, or prostate cancer, without identification of single biomarkers. MALDI-TOF MS, for example, offers a simple approach for fast and reliable protein profiling, especially by using carrier materials with various physical and chemical properties, in combination with a MALDI matrix. This approach is referred to as materialenhanced laser desorption/ionization (MELDI). In this paper, we report the development and application of derivatized carrier materials [cellulose, silica, poly(glycidyl methacrylate/divinylbenzene) (GMA/DVB) particles, and diamond powder] for fast and direct MALDI-TOF MS protein profiling. The applicability of MELDI for rapid protein profiling was evaluated with human serum samples. These carriers, having various hydrophobicities, resulted in characteristic mass fingerprints, even if all materials were derivatized with iminodiacetic acid (IDA) to yield an immobilized metal affinity chromatography (IMAC) functionality. Our study demonstrates that analyzing complex biological samples, such as human serum, by employing different MELDI carrier materials yielded type-and size-dependent performance variation. T he quest to diagnose and identify diseases at early stages depends mainly on the accurate determination of the marker entities in the biological fluids. These marker entities are normally very low concentrated [1], and highly sensitive methods are required to bind them effectively from the biosamples and to measure them with matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS) [2]. MALDI mass spectrometry, in recent times, has proven to be an authentic technique to analyze peptides and proteins [3,4]. These biomolecules out of the complex biofluids like serum are difficult to ionize and thus, bring into time of flight (TOF) because of the complexity of the sample and the suppressing nonvolatile salts [5]. The aforementioned problems are tackled by another technique introduced years ago, namely, surface-enhanced laser desorption/ionization time of flight mass spectrometry (SELDI-TOF MS), for the detection of several peptides and proteins from complex biological specimens [6 -8]. This affinity-based method utilizes selective adsorption of proteins on various chromatographic surfaces to reduce sample complexity [9,10]. Spectra generated by SELDI-TOF MS usually show limited peak and binding capacity due to the smaller surface area of the plane protein chip [11]. Limitations of SELDI are also associated with the lower mass resolution of the applied MS instrument that

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“…A typical example is cyanogen bromide (CNBr)-activated Sepharose (Nisnevitch and Firer, 2001), but various alternatives are available [tosyl and epoxy activated beads] (Hage, 1998;Larsson, 1984). This simple, straightforward methodology is recommended when the amount of antibody available is not expected to be a limiting factor, e.g.…”

Section: Random Chemical Attachmentmentioning

confidence: 99%