Alumina-phosphate complexes for immobilization of biomolecules

Ma, Che; Previero, A.

doi:10.1016/0003-2697(89)90080-8

Cited by 53 publications

(23 citation statements)

References 28 publications

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“…And the excellent phosphorylated protein adsorption property of AGNP may be attributed to the large specific surface area (137.8 m 2 g -1 , Table S2 in ESI †) and affinity-like chromatography between aluminium hydroxide and phosphate group. 29 In addition, the adsorption isotherms were fitted well to the Langmuir model (Table 1 and Fig. S4 in ESI †).…”

Section: Please Do Not Adjust Marginsmentioning

confidence: 87%

Aluminium glycinate functionalized silica nanoparticles for highly specific separation of phosphoproteins

Liu

Zheng

et al. 2015

J. Mater. Chem. B

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Selective separation of intact phosphoproteins from complex biological samples is essential for the ongoing top-down phosphoproteomics, but challenges still remain. Herein, aluminium hydroxide functionalized silica nanoparticles (denoted as AGNP) was synthesized by a facile approach and applied for specific capture of phosphoproteins. The selectivity and binding capacity of AGNP were evaluated by using caseins (α-casein and β-casein) as phosphoproteins and nonphosphoproteins (bovine haemoglobin, bovine serum albumin, horseradish peroxidase, myoglobin and lysozyme) as nonphoproteins. The results indicated that the AGNP showed high bind-ing capacity and selectivity for phosphpproteins (αcasein 1190 mg g -1 and β-casein 1060 mg g -1 ). In addi-tion, the AGNP can be used to selectively capture and enrich phosphpproteins from protein mixture and drinking milk samples. The good results demonstrate the potential of the AGNP in phosphoproteomics analysis.Aluminium hydroxide functionalized silica nanoparticles was synthesized by a facile approach and successfully applied for specific capture of phosphoproteins from complex sample.

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Section: Please Do Not Adjust Marginsmentioning

confidence: 87%

Aluminium glycinate functionalized silica nanoparticles for highly specific separation of phosphoproteins

Liu

Zheng

et al. 2015

J. Mater. Chem. B

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“…Alumina is widely used as a substrate material for copious biomedical and biotechnological applications, e.g. in protein separation and purification systems [25], biosensors [25], biocatalysis [26,27] or drug carrier applications [28]. Surface functionalization with sulfonic acids is often used to stabilize inorganic particles in biological media, or to introduce ion exchange [29] or catalytic properties [30].…”

Section: Introductionmentioning

confidence: 99%

Controlling protein–particle adsorption by surface tailoring colloidal alumina particles with sulfonate groups

et al. 2013

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“…Because of this wide application, protein adsorption to aluminium hydroxide has been studied in considerable detail and some of those studies also investigate the binding behaviour of phosphorylated proteins to aluminium hydroxide (Kato et al, 1994;Chang et al, 1997;Shi et al, 2001b;Iyer et al, 2003). In addition, aluminium oxide, a close relative of aluminium hydroxide, has been reported to exhibit a high and selective attraction to phosphorylated biomolecules (Colettipreviero and Previero, 1989). The conclusion of these studies is that aluminium hydroxide and oxide both have a high affinity for phosphorylated biomolecules and that the affinity towards phosphate is considerably higher than for sulfate or nitrate.…”

Section: Aluminum Oxide and Hydroxidementioning

confidence: 96%

Multisite Protein Phosphorylation in Plants - Technical Considerations and Biological Implications

Wolschin¹,

Chen

Weckwerth

2006

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Since protein phosphorylation was accepted to play a key role in cellular metabolism the investigation of this important posttranslational modification has gained ever-growing interest of researchers. However, until recently, technical challenges have made large scale studies on protein phosphorylation impossible. With dramatic improvements in both phosporylated peptides/proteins enrichment methods and in the selectivity and resolving power of mass spectrometry based techniques, the main challenges have been addressed and large scale protein phosphorylation studies are now being conducted. These technical advancements have also opened the door for the more accurate determination of actual protein phosphorylation sites. Consequently, another important aspect of this prominent signalling event can be investigated: proteins possess several phosphorylation sites and it is assumed that many of them have distinct regulatory function. While these processes are under thorough investigation in animals, protein phosphorylation in plants is still a developing field. This is particularly surprising in light of the enormous number of predicted protein kinases in the Arabidopsis thaliana genome exceeding apparently the complexity of animal systems.In this review, we illustrate the advantages and drawbacks of methods currently used for studying phosphorylation with an emphasis on phosphoprotein/peptide enrichment and mass spectrometry. We then describe how these methods can be used to reveal the biological importance of multisite protein phosphorylation in plants.

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Alumina-phosphate complexes for immobilization of biomolecules

Cited by 53 publications

References 28 publications

Aluminium glycinate functionalized silica nanoparticles for highly specific separation of phosphoproteins

Aluminium glycinate functionalized silica nanoparticles for highly specific separation of phosphoproteins

Controlling protein–particle adsorption by surface tailoring colloidal alumina particles with sulfonate groups

Multisite Protein Phosphorylation in Plants - Technical Considerations and Biological Implications

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