Use of hydrophilic interaction chromatography for the study of tyrosine protein kinase specificity

Ernould, Anne-Pascale; Ferry, Gilles; Genton, Annie; Alpert, Andrew J.

doi:10.1016/0378-4347(92)80546-3

Cited by 37 publications

(20 citation statements)

References 14 publications

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“…Certain solutes seem to be more affected than others. [54,233,266]; pyridylaminated sialo sugar chains [219]; quaternary ammonium compounds [133]; small polar compounds in food analysis by HILIC/ESI-MS [155]; hydroxybenzoate saxitoxin analogs in dinoflagellates [160]; chitine fragments [198]; cyanobacterial toxins by HILIC/MS [164]; 1-deoxynojirimycin in mulberry leaves [150]; polar compounds contributing to umami taste and mouth-drying oral sensation of morel mushrooms [156]; elucidation of yeast sulfur metabolism [253]; PSP toxins [166,165,167]; monosaccharides [227,267]; identification of a bitter inhibitor [157] Peptides, nucleic acids, and other polar compounds [13]; peptides [67]; tyrosine protein-kinase specificity [234]; desalting of electroeluted proteins [241]; glycopeptides [268]; site-specific glycosylation microheterogeneity in recombinant human interferon-c [269]; urea, allantoin and lysine pyroglutamate in cosmetic samples [134]; glucosinolates in vegetables [201]; folates in human plasma by HILIC/ MS/MS [137]; citrulline in dried blood spots [138]; SPE enrichment of avoparcin from kidney samples [254]: Ionic compounds by pressurized flow CEC [270]; sucrose in a plasma-derived process solution [271]; glycoalkaloids in transgenic potatoes [104]; glycopeptide microheterogeneity [272] Peptides [67,68,276]; amphipathic a-helical peptides …”

Section: Underivatized Silicamentioning

confidence: 99%

“…The predicted retention times had a reasonably good fit (r 2 = 0.94) and the observed retention times were generally within 10 -20% of those predicted. Boutin et al [234] separated phosphorylated peptides from c-32 P-ATP and inorganic 32 P in tyrosine protein kinase assays by a poly(2-hydroxyethyl aspartamide) silica, which was used both for sample preparation by SPE and for HPLC in HILIC mode. Peptide separations by HILIC were recently reviewed by Yoshida [22].…”

Section: Amino Acids and Peptidesmentioning

confidence: 99%

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Hydrophilic interaction chromatography

Hemström

Irgum²

2006

J of Separation Science

1,076

818

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Separation of polar compounds on polar stationary phases with partly aqueous eluents is by no means a new separation mode in LC. The first HPLC applications were published more than 30 years ago, and were for a long time mostly confined to carbohydrate analysis. In the early 1990s new phases started to emerge, and the practice was given a name, hydrophilic interaction chromatography (HILIC). Although the use of this separation mode has been relatively limited, we have seen a sudden increase in popularity over the last few years, promoted by the need to analyze polar compounds in increasingly complex mixtures. Another reason for the increase in popularity is the widespread use of MS coupled to LC. The partly aqueous eluents high in ACN with a limited need of adding salt is almost ideal for ESI. The applications now encompass most categories of polar compounds, charged as well as uncharged, although HILIC is particularly well suited for solutes lacking charge where coulombic interactions cannot be used to mediate retention. The review attempts to summarize the ongoing discussion on the separation mechanism and gives an overview of the stationary phases used and the applications addressed with this separation mode in LC.

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Section: Underivatized Silicamentioning

confidence: 99%

Section: Amino Acids and Peptidesmentioning

confidence: 99%

Hydrophilic interaction chromatography

Hemström

Irgum²

2006

J of Separation Science

1,076

818

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“…HILIC proved to be very useful in separating a range of polar peptides. Boutin et al (1992) used HILIC for the study of tyrosine protein kinase specificity. Using a polyhydroxyethyl A column, phosphorylated peptide, nonphosphorylated peptide, ATP, and inorganic phosphate were separated.…”

Section: Hydrophylic Interaction Chromatographymentioning

confidence: 99%

Chromatographic Techniques for the Characterization of Proteins

Holthuis¹,

Driebergen²

1995

Pharmaceutical Biotechnology

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“…As a constant shared by many TPKs, a requirement for acidic residues in the vicinity of the tyrosine residue was found for most of the substrates. A close analysis of acidic peptides was made possible by our new method of measurement using hydrophilic chromatography [42].…”

Section: Tpkmentioning

confidence: 99%

Purification and characterization of the major tyrosine protein kinase from the human promyelocytic cell line, HL60

Ernould¹,

Ferry²,

Barret³

et al. 1993

European Journal of Biochemistry

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The major tyrosine protein kinase from HL60 (a human non-differentiated promyelocytic cell line) has been purified almost to homogeneity as judged by silver-stained SDS/PAGE. The procedure involved four chromatographic steps : DEAE-Sepharose, casein-agarose, cibacron-blue -agarose and hexyl-agarose. The purification resulted in more than 1000-fold enrichment in angiotensin I1 phosphorylation activity. A gel-sizing experiment, labeling with [35S]ATP [ys] and autophosphorylation of the enzyme in the presence of [Y-~~PIATP, all led to the identification of a single protein species with a molecular mass of about 40 kDa. Western blot experiments showed that this protein does not belong to the src family and is not related to the abl andfes oncogene products. Phosphorylation of angiotensin 11 and casein by this 40-kDa human promyelocytic kinase was stimulated by high ionic strength especially from class IA metal salts. The K, for ATP was 2 pM and the V,, 3.1 nmol min-' . mg-' using angiotensin fI as a substrate. The kinase requires the presence of either Mn2+ or Mg2+ for full activity and utilizes ATP or dATP but not GTP as phosphate donor. Based on numerous biochemical observations, it was possible to demonstrate that kinase is different from any other tyrosine protein kinases described in the literature. This 40-kDa protein was used as a molecular tool for testing some tyrosine protein kinase inhibitors described in the literature. It is one of the rare tyrosine protein kinases purified from human cancer cells to date.Protein phosphorylation plays a key role in the control of cellular communication [l]. Amongst the enzymes catalyzing the phosphorylation of other proteins (on specific amino acid residues), the tyrosine protein kinases (TPK) are known to be involved in the regulation of growth signal transmission and cellular transformation [2], according to their functional similarity to growth factor receptors and oncogene products [3]. A growing number of TPK(s) have been identified, mostly from molecular cloning of protein kinase genes rather than through enzyme purification [4]. TPK(s) can be classified in three categories [5][6][7]: (a) the transmembrane-receptor-associated TPK activity as found, for instance, in epidermal growth factor EGF, platelet growth factor PDGF and insulin receptors; (b) the TPK(s) linked to the inner face of the plasma membrane represented by the src family with src, yes, f g r , f m , lyn, hck, lck and blk oncogene products which are all myristoylated [8] and (c) the cytosolic TPK(s) with major representatives being abl and fes/fgr oncogene products.From a molecular pharmacological point of view, TPK(s) are new targets for inhibitors [9] To understand the cellular function of these TPKs one needs to characterize them on the basis of classical biochemistry studies (purification, molecular identification, kinetic data, effect of modulators, etc.). A major example was recently provided by Litwin et al. [24] and Cheng et al. [25], on a TPK specifically phosphorylating the p34cdc2 kinase ...

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Use of hydrophilic interaction chromatography for the study of tyrosine protein kinase specificity

Cited by 37 publications

References 14 publications

Hydrophilic interaction chromatography

Hydrophilic interaction chromatography

Chromatographic Techniques for the Characterization of Proteins

Purification and characterization of the major tyrosine protein kinase from the human promyelocytic cell line, HL60

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