Anion exchange chromatography of 99mTc(Sn)-MDP complexes: Influence of eluent composition, determination of void volume and charge of the main component

Huigen, Y.M.; Tji, T.G.; Gelsema, W.J.; Ligny, C.L. De

doi:10.1016/0883-2889(88)90088-3

Cited by 8 publications

(2 citation statements)

References 6 publications

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“…Ion exchange chromatography separate peptides based primarily on ionic charge. , Therefore, many of phosphopeptides can not be remained in the SCX and SAX chromatography column due to their charge state. At pH 2.7, Gygi and colleagues predicted that 68% of in silico tryptic peptides in the human database have a net charge of 2+, any of these peptides would still have a net charge state of 1+ after the addition of a single phosphate, these peptides would bind to SCX column when loaded with pH 2.7 loading buffer.…”

Section: Resultsmentioning

confidence: 99%

“…More than 1200 unique phosphopeptides were identified in both the unbound fraction of SCX and SAX, but the chemical feature of phosphopeptides in the unbound fraction of SCX/SAX is significantly different because SCX and SAX chromatography separate peptides based primarily on ionic charge. , Acidic and multiply phosphorylated peptides dominated in the unbound fraction of SCX, whereas more basic and singly phosphorylated peptides were contained in the unbound fraction of SAX. The distributions of theoretical pI value of identified phosphopeptides in the unbound fraction are plotted in Figure A.…”

Section: Resultsmentioning

confidence: 99%

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Comprehensive Profiling of Phosphopeptides Based on Anion Exchange Followed by Flow-Through Enrichment with Titanium Dioxide (AFET)

et al. 2010

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For large-scale analysis of phosphorylation at proteome-wide scale, a variety of affinity-based strategies have been developed to enrich phosphopeptide. Because each method differed in their specificity of isolation, the global and unbiased enrichment of phosphopeptides remains a major technical challenge in phosphoproteomics. In the present work, we demostrate that the phosphopeptide enrichment method based on an online continuous pH gradient in a strong anion exchange column (SAX method) is highly complementary to the method based on titanium dioxide (TiO2) affinity enrichment. Moreover, we found that the flow-through fraction of either SAX or SCX is very phosphopeptide-rich, which necessitates further analysis by complementary method. Here, we developed a comprehensive phosphopeptides profiling strategy based on anion exchange followed by flow-through enrichment by TiO2 (AFET). In this strategy, SAX method was used as the first separation/enrichment step, which was online coupled with LC-MS/MS. The phosphopeptides in the SAX flow-through fraction were further enriched with TiO2. As a result, a more comprehensive, less biased phosphoproteome was aquired. Careful comparison of four different combination strategies reveal that the AFET method showed the advantages of more identified phosphopeptides, less mass spectrometry analysis time, as well as simple and automatic process step. It is well-suited for robust and reproducible phosphoproteomics, especially in the case of small amounts of sample.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Comprehensive Profiling of Phosphopeptides Based on Anion Exchange Followed by Flow-Through Enrichment with Titanium Dioxide (AFET)

et al. 2010

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Effect of the eluent composition in gel chromatography of99mTc (Sn)-methylene diphosphonate

Vučina

1995

Journal of Radioanalytical and Nuclear Chemistry Letters

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Quality control and clinical application of two bone imaging99mTc radiopharmaceuticals

Ayranov

Strezov

Jordanova

et al. 1999

J Radioanal Nucl Chem

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The radiochemical purity of MDP and HEDP has been determined by means of gel chromatography on Sephadex and thin layer chromatography on plastic foil silica gel. The comparison of the two radiopharmaceuticals shows equal level of complex formation with 99mTc. The biodistribution demonstrated that the application of HEDP allows earlier scanning than MDP. MDP and HEDP show equal effectivity during the clinical investigations. There is no significant difference in the radiochemical purity within six hours after the reconstitution of the freeze-dried kits. HEDP kit demonstrates shorter period of accumulation and equivalent complex formation levels, so it can be used in routine nuclear medicine diagnostics together with MDP kit.

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Anion exchange chromatography of 99mTc(Sn)-MDP complexes: Influence of eluent composition, determination of void volume and charge of the main component

Cited by 8 publications

References 6 publications

Comprehensive Profiling of Phosphopeptides Based on Anion Exchange Followed by Flow-Through Enrichment with Titanium Dioxide (AFET)

Comprehensive Profiling of Phosphopeptides Based on Anion Exchange Followed by Flow-Through Enrichment with Titanium Dioxide (AFET)

Effect of the eluent composition in gel chromatography of99mTc (Sn)-methylene diphosphonate

Quality control and clinical application of two bone imaging99mTc radiopharmaceuticals

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