Method and Apparatus for Measuring Protein Post-Translational Modification
Inactive Publication Date: 2009-04-02
ICAGEN INC
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The analysis of post-translational modifications often requires labor intensive sample
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example 1
[0035]NAD+ kinase served as the acceptor chemical and as a controller chemical. Adenosine triphosphate served as the donor chemical.
[0036]Magnesium chloride and acetic acid served as controller chemicals.
[0037]Phosphorylated NAD kinase served as the acceptor product. Adenosine diphosphate served as the donor product. A solution was prepared by combining 100 microliters of a solution of NAD kinase [880 micromolar] in water with a 200 microliters of a solution of adenosine triphosphate [5 millimolar], magnesium chloride [10 millimolar], tris(hydroxymethyl)aminomethane buffer [100 millimolar, pH 7.5] in water (FIG. 1, Box 1). The reaction was allowed to incubate for 10 seconds, after which 200 microliters of a solution of 5% acetic acid in water was added (FIG. 1, Box 2). The acceptor product was separated from the adenosine triphosphate and adenosine diphosphate using a Microcon 3000 molecular weight cut off (MWCO) ultrafilter, available from Millipore Corporate Headquarters, 290 Conc...
example 2
[0038]A set of peptides having the formula: polystyrene bead-LINKER-cysteine-1-xxx1-xxx2-xxx3-xxx4-cysteine2, where xxx1, xxx2, xxx3, and xxx4 are independently selected from the amino acids {alanine, arginine, asparagine, aspartic acid, glutamine, glutamic acid, glycine, histidine, isoleucine, leucine, lysine, phenylalanine, proline, serine, threonine, tryptophan, tyrosine, and valine} served as the donor chemical. “Polystyrene bead-LINKER” refers to AM resin such as available from Rapp Polymere GmbH, Emst-Simon-Str. 9, D 72072 Tübingen, Germany. Water served as the acceptor chemical. Trypsin and K2PtCl4 served as controller chemicals. The peptides having the formula: polystyrene bead-LINKER-cysteine1-xxx1-xxx2-xxx3-xxx4-CO2H served as the donor product, where xxx1, xxx2, xxx3, and xxx4 are independently selected from the amino acids {alanine, arginine, asparagine, aspartic acid, glutamine, glutamic acid, glycine, histidine, isoleucine, leucine, lysine, phenylalanine, proline, seri...
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Abstract
The present invention includes a method for analyzing reactions. The method includes the steps of providing a solution of at least one acceptor chemical and at least one donor chemical. The donor chemical is capable of donating a chemical moiety to the acceptor chemical. The solution further includes at least one controller chemical that affects the reaction between the donor chemical and the acceptor chemical. The solution is then incubated so that a portion of the acceptor chemical reacts with the donor chemical to form an acceptor product. Unreacted donor chemical is separated from the acceptor product. The acceptor product or the donor chemical is then measured using X-ray fluorescence. Another aspect of the present invention includes a method for analyzing protein function. The method includes the steps of providing a solution of at least one acceptor chemical and at least one donor chemical. The donor chemical is capable of donating a chemical moiety to the acceptor chemical. The donor chemical includes a functional group selected from ester, anhydride, imide, acyl halide, and amide. The solution is then incubated so that a portion of the acceptor chemical reacts with the donor chemical to form an acceptor product. Unreacted donor chemical is separated from the acceptor product. The acceptor product or the donor chemical is then measured using X-ray fluorescence. Yet another aspect of the present invention includes a method for analyzing protein function. The method includes the steps of providing a solution of at least one acceptor chemical and at least one donor chemical. The solution is then incubated so that a portion of the acceptor chemical reacts with the donor chemical to form an acceptor product. Unreacted donor chemical is separated from the acceptor product. The acceptor product or the donor chemical is then measured using X-ray fluorescence. An additional analytical method is also used to measure either the acceptor product or the donor chemical.
Description
RELATED APPLICATIONS[0001]This application claims the priority of U.S. Provisional Patent Application 60 / 995,997 entitled “Method and Apparatus for Measuring Protein Post-Translational Modification,” which was filed on Sep. 28, 2007, incorporated by reference herein.FIELD OF THE INVENTION[0002]The present invention relates to the analysis of protein function.BACKGROUND OF THE INVENTION[0003]Post-translational modifications are chemical changes to proteins that occur after the primary structure of the protein has been completed via translation. Post-translational modifications include, but are not limited to, phosphorylation, dephosphorylation, proteolysis, protein ligation, glycosylation, sulfation, methylation, and ubiquitination.[0004]Post-translational modifications influence protein behavior. For example, insulin is formed by the post-translational modification of proinsulin, which itself is formed by the post-translational modification of preproinsulin. The post-translational a...
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