Fractionation of membrane proteins on immobilized lectins by high-performance liquid affinity chromatography

Renauer, Doris; Oesch, Franz; Kinkel, J.N.; Unger, Klaus K.; Wieser, Raimund

doi:10.1016/0003-2697(85)90198-8

Cited by 29 publications

(8 citation statements)

References 14 publications

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“…The accessibility of the binding sites was calculated according to Eq. [3] to be A ϭ 82%. This value is very high, even more when one takes into account that ASF is a large molecule.…”

Section: A͓%͔mentioning

confidence: 97%

“…The lectin (hemagglutinin) of Ricinus communis (RCA 120 ) 3 is of special interest because of its high affinity and particular specificity for glycoconjugates containing terminal ␤-D-galactosyl residues (7,8). This lectin (MW ϭ 120,000 g/mol) is composed of two A-type and two B-type chains and has two identical and independent binding sites for galactose per RCA molecule (1,9).…”

mentioning

confidence: 99%

“…Immobilized on solid matrices lectins can be used for biospecific affinity separations (3)(4)(5)(6). Lectin affinity chromatography provides a powerful method for purification of oligosaccharides and glycoconjugates (e.g., glycoproteins or glycolipids) that often represent pharmaceutical active compounds.…”

mentioning

confidence: 99%

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Preparation and Evaluation of Ricinus communis Agglutinin Affinity Adsorbents Using Polymeric Supports

Cartellieri¹,

Helmholz²,

Niemeyer³

2001

Analytical Biochemistry

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“…The accessibility of the binding sites was calculated according to Eq. [3] to be A ϭ 82%. This value is very high, even more when one takes into account that ASF is a large molecule.…”

Section: A͓%͔mentioning

confidence: 97%

mentioning

confidence: 99%

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Preparation and Evaluation of Ricinus communis Agglutinin Affinity Adsorbents Using Polymeric Supports

Cartellieri¹,

Helmholz²,

Niemeyer³

2001

Analytical Biochemistry

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“…In this method, a WGA column was able to separate the liver-and bone-derived isoenzymes of alkaline phosphatase in human serum [108], giving better resolution than a similar low-performance column [109]. Con A has also been used with silica and HPAC for the study of glycoproteins such as ovalbumin [110], horseradish peroxidase [111], glucose oxidase [111], and membrane glycoproteins [112,113]. [118][119][120].…”

Section: Use Of Silica and Affinity Ligands For Direct Detectionmentioning

confidence: 99%

Applications of silica supports in affinity chromatography

Schiel

Mallik

Soman

et al. 2006

J of Separation Science

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The combined use of silica-based chromatographic supports with immobilized affinity ligands can be used in many preparative and analytical applications. One example is the use of silica-based affinity columns in HPLC, giving rise to a method known as high-performance affinity chromatography (HPAC). This review discusses the role that silica has played in the development of affinity chromatography and HPAC and the applications of silica in these methods. This includes a discussion of the types of ligands that have been employed with silica and the methods by which these ligands have been immobilized. Various formats have also been presented for the use of silica in affinity chromatographic methods, including assays involving direct or indirect analyte detection, on-line or off-line affinity extraction, and chiral separations. The use of silica-based affinity columns in studies of biological systems based on zonal elution and frontal analysis methods will also be considered.

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“…Moreover, lectins can be immobilized in distinct solid supports (e.g. silica (157), agarose (158) or sepharose (159)), monolithic columns (160), and in microdimensional systems (146,153,156,161,162), including magnetic particles (142,153). These magnetic beads coupled to lectins have been recently used for capturing glycoproteins in complex biological samples, taking advantage of their high surface area and high mobility in solution (142,161).…”

Section: Glycosylationmentioning

confidence: 99%

Post-translational Modifications and Mass Spectrometry Detection

Silva

Vitorino

Domingues

et al. 2013

Free Radical Biology and Medicine

114

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In this review, we provide a comprehensive bibliographic overview of the role of mass spectrometry and the recent technical developments in the detection of post-translational modifications (PTMs). We briefly describe the principles of mass spectrometry for detecting PTMs and the protein and peptide enrichment strategies for PTM analysis, including phosphorylation, acetylation and oxidation. This review presents a bibliographic overview of the scientific achievements and the recent technical development in the detection of PTMs is provided. In order to ascertain the state of the art in mass spectrometry and proteomics methodologies for the study of PTMs, we analyzed all the PTM data introduced in the Universal Protein Resource (UniProt) and the literature published in the last three years. The evolution of curated data in UniProt for proteins annotated as being posttranslationally modified is also analyzed. Additionally, we have undertaken a careful analysis of the research articles published in the years 2010 to 2012 reporting the detection of PTMs in biological samples by mass spectrometry.

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Fractionation of membrane proteins on immobilized lectins by high-performance liquid affinity chromatography

Cited by 29 publications

References 14 publications

Preparation and Evaluation of Ricinus communis Agglutinin Affinity Adsorbents Using Polymeric Supports

Preparation and Evaluation of Ricinus communis Agglutinin Affinity Adsorbents Using Polymeric Supports

Applications of silica supports in affinity chromatography

Post-translational Modifications and Mass Spectrometry Detection

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