PolySulfoethyl

PolySULFOETHYL A spartamide

- for cation-exchange of peptides

This strong cation-exchange (SCX) material was developed specifically for HPLC of peptides.At pH 2.7-3.0, peptides lose their (-) charges, and have net (+) charge. They can be retained by a SCX column such as PolySULFOETHYL A.

With a salt gradient, peptides elute in order of increasing number of basic residues. Thus, the  selectivity complements that of RPC.

The capacity is several times greater than that of SCX and RPC, used in sequence, will yield sequenceable peptides from most crude mixtures.

When to use SCX:

  1. Mapping of peptide digests (tryptic, V8, CNBr etc) and isoforms.
  2. Purification of synthetic peptides.
  3. Isolation of natural peptides from crude extracts.
  4. Specific isolation of disulfide-linked peptides from digests.
  5. Specific isolation of C-terminal peptides.
  6. Assay of N- and C-terminal variant peptides and peptides with blocked termini.
  7. Quality control assays requiring a method orthogonal to RPC.

Most other SCX columns are based on sulfopropyl- (SP-) groups. Hydrophobic interactions are significant with such groups. This often results in poor recovery and efficiency with hydrophobic peptides. By contrast, PolySULFOETHYL A is based on sulfoethyl- groups, and recovery of peptides is generally high or quantitative.                                                     

Papers  on PolySULFOETHYL Aspartamide

Subject

S1.  Alpert & Andrews, J. Chromatogr. 443(1988) 85

Description  of PolySULFOETHYL A . and SCX of peptides

S2.  Crimmins et al., J. Chromatogr. 443 (1988) 63

SCX  of peptides

S3.  Andrews, Peptide Res. 1 (1988) 93

Ion-exchange  HPLC of peptides.

S4.  Crimmins et al., Biochem. Biophys. Res.Commun. 156 (1988) 910.

SCX  analysis of deblocking of N-terminal pyro-Glu- peptides

S5.  Crimmins et al., Anal. Biochem. 176 (1989) 255

Peptide  mapping of V8 digests by SCX.

S6.  Schlabach et al., Techniques in Protein Chem. 1 (Academic Press  ; 1989) 497

Peptide  mapping of Asp-N digest.

S7.  Crimmins, Peptide Res. 2 (1989) 395.

SCX  of disulphide-linked peptides

S8.  Kolbe et al., J. Chromatogr. 476 (1989) 99.

Purif.  of recombinant p18 protein fr om HIV-1 virus

S9.  Andrews, Current Res. Protein Chem (Academic Press ; 1990) 95.

Selective  isolation of disulphide-linked peptides from tryptic digests

S10.  Iadarola et al., J. Chromatogr. 512 (1990) 165.

Albumin  variant digests by CNBr, trypsin, and V8 ; SCX vs. RPC.

S11.  Sandy et al., J. Biol. Chem. 265 (1990) 21108.

Isoln.  of disulphide-linked peptides from aggregating cartilage  proteoglycan.

S12.  Guarino & Phillips, Amer. Lab. 23 (1991) 68.

SCX-HPLC  of peptides as a prepar. adjunct to CZE

S13.  Swiderek et al., Eur. J. Biochem. 190 (1990) 575.

V8  digest of Troponin T ; mapping sites of phosphorylation

S14.  Alpert, HPLC of Peptides and Proteins (Mant & Hodges, eds.).  (CRC Press ; 1991) 187.

IEX  of peptides.

S15.  Crimmins, Techniques in Protein Chem. III (Academic Press :  1992) 171

SCX  vs. CZE of synthetic peptides.

S16.  Zhu et al., J. Chromatogr. 548 (1991) 13

HILIC  of peptides (same ref. as H2).

S17.  Zhu et al., J. Chromatogr. 594 (1992) 75

SCX-HILIC  of peptides vs. RPC

S18.  Przysiecki et al., Protein Expression Purif. 3 (1992) 185

Purif.  of recombinant antistasin with a . preproleader sequence (same  ref. as H6)

S19.  Clogston et al., Anal. Biochem. 202 (1992) 375

Analysis  of rG-CSF isoforms

S20.  Schmeltzer et al., J. Neurochem. 59 (1992) 1675.

Isoln.  & anal. of rh-Nerve Growth Factor

S21.  Hempel et al., Comp. Biochem. Physiol. 102B (1992) 791

SCX  of tryptic digest of human liver . glutamic Semialdehyde Dehydrogenase.

S22.  Churchill et al., Biochemistry 31 (1992) 3793.

SCX  of tryptic digest of rat liver D-beta-hydroxybutyrate dehydrogenase.

S23.  Moore et al., Proc. Natl. Acad. Sci. 90 (1993) 1354.

Isoln. of squalamine (a steroidal antibiotic).

S24.  Kieliszewski et al., Plant Physiol. 98 (1992) 919.

Purif.  of hydroxyproline-rich glycoprotein from Douglas fir.

S25.  Kieliszewski et al., Plant Physiol. 99 (1992) 538.

Purif.  of His-rich, arabinogalactan protein from corn (maize).

S26.  Fong et al., Plant Physiol. 99 (1992) 548.

Purif.  of gymnosperm protein with serine tetrahydroxyproline motif.

S27.  Longo et al., Cell Regulation 1 (1990) 189.

Purif.  of synthetic peptide fragments of Nerve Growth Factor which  inhibit NGF.

S28.  Hisatsune et al., Biosci. Biotech. Biochem. 56 (1992) 1616

Purif.  of a CNBr digest of casein.

S29.  Nichols, Molec. Cell. Neurosci. 3 (1992) 342

Isoln.  of Drosophila Drosulfakinin Neural Peptide gene product, DSK-1.

S30.  Nichols, J. Mol. Neurosci. 3 (1992) 213.

Isolation  of Drosophila neural peptides

S31.  Tanasijevic et al., J. Biol. Chem. 268 (1993) 18157

Isolation  of phosphorylated fragments of Insulin Receptor Substrate  (IRS-1).

S32.  Dolmer & Sottrup-Jensen, FEBS Letters 315 (1993) 85

Isoln.  of disulphide-linked peptides from human complement component  C3b.

S33.  Gorman & Shiell, J. Chromatogr. 646 (1993) 193.

Selective  isoln. of C-terminal and blocked N-terminal peptides from viral proteins.

S34.  Dong et al., J. Biol. Chem. 269 (1994) 6753.

Determination  of disulphide bonds in von Willebrand Factor multimers.

S35.  Walker, Poster 272-T, Protein Society Symp. (7/94).

Assay  of Growth Hormone-Releasing Factor by mixed SCX-HILIC.

S36.  Crimmins, Meth. Mol. Biol. 36 (1994) 53.

SCX  in synthetic peptide analysis.

S37.  Hempel et al., Protein Sci. 3 (1994) 1074

Purif.  of peptides for sequencing from digest of UDP-glucose dehydrogenase.

S38.  Crimmins et al., Anal. Biochem. 226 (1995) 355

Disulf.-linked  peptides : SCX & MALDI-MS

S39.  Fang et al., J. Chromatogr. A729 (1996) 49.

Effect  of temperature on protein  retention times in cation-exchange.

S40.  Fang et al., J. Chromatogr. A729 (1996) 67.

Effect  of temperature on protein bandwith in cation-exchange.

S41.  Smith and Hanly, in Irvine and Williams (eds.),  Neuropeptide  Protocols (Methods in Molec. Biology vol. 73), Human Press Inc.,  Totowa, NJ, 1996, pg. 75.

a) Protocol  for SCX of peptides

b) Purif. of crude synthetic Calcitonin

Gene-Related Peptide (8-37).

S42.  Joyal et al., Biochemistry 35 (1996) 6267

Identification  of phosphorylation sites in calmodulin.

S43.  Bendixen et al., J. Biol. Chem. 270 (1995) 17929

Isoln.  of plasminogen fragments covalently linked (Glu-Lys) by trans-  glutaminase treatment.

S44.  Mant & Hodges, Meth. Enzymol. 271 (1996) 3

SCX  of peptides : Hydrophilic & hydrophobic mixed-mode effects.

S45.  Yarus et al., Proc. Natl. Acad Sci. 93 (1996) 14118.

Purif.  of bovine tracheal antimicrobial peptide (a beta-defensin)  from transgenic mouse milk.

S46.  Cole et al., J. Biol. Chem. 272 (1997) 12008.

Isoln.  of pleurocidin, an antimicrobial peptide from flounder  skin.

S47.  Crimmins et al., Anal. Chim. Acta 352 (1997) 21.

SCX-HPLC  as a tool for characterization and purif. of peptides.

S48.  Link et al., Nature Biotechnol. 17 (1999) 676.

Proteome  analysis: SCX-RPC capillaries for direct MS/MS analysis  of protein complexes.

S49.  Tseng et al., J. Biol. Chem. 271 (1996) 23992.

Purification  of human type II phospholipase A2 from CHO cells  (SCX-RPC  sequence).

S50.  John et al., Proc. Natl. Acad. Sci. 94 (1997) 10178.

Isolation  via SEC-SCX-RPC of a 17-residue peptide mediating glycolipid-induced  tobacco protoplast proliferation in vitro.

S51.  Louie and Meade, Proc. Natl. Acad. Sci. 95 (1998)

Purification  of cobalt complexes of zinc finger peptides

S52.  Giblin et al., Proc. Natl. Acad. Sci. 95 (1998) 12814.

Purification  of complex of rhenium with alpha-MSH.

S53.  Hekman et al., Pharm. Res. 15 (1998) 650.

Isolation  and identification of degradation products of pramlintide (an amylin analogue).

S54.  Hekman et al., J. Pharm. Biomed. Anal.20 (1999) 763.

Isolation  and identification of cyclic imide and deamidation products  of pramlintide

S55.  Ayad et al., J. Dental Res.79 (2000) 976.

Isolation  of 19 basic, proline-rich peptides from human saliva; relationship  to dental  decay

S56.  Gygi et al., Proc. Natl. Acad. Sci. 97 (2000) 9390.

Proteomics  tools: analysis of 2D gel spots of yeast proteins using  a trypsin-SCX-RPC- MS/MS sequence.

S57.  Davis et al., Poster  196, 48th ASMS Conference (June 2000).

Proteomics analyses using a SCX-RPC- MS/MS setup.

S58.  Gygi et al., Curr. Opinion Biotechnol. 11 (2000) 396.

Review  of ICAT and proteomics.

S59.  Adermann et al., Protein Sci. 8 (1999) 810.

Isolation  from human urine of SLURP-1, a member of the Ly-6/uPAR protein  superfamily.

S60.  Blitvich et al., Virus Res. 60 (1999) 67.

Selective  isolation of C-terminal tryptic peptides from flavivirus NS1  protein.

S61.  Goodrum et al., Phytochem. 54 (2000) 99.

Purification  of chymotryptic peptides of gum arabic glycoprotein via a SCX-RPC  sequence.

S62.  Yoshida et al., Brain Res. 894 (2001) 46.

Purification  of recombinant midkine neurotrophic factor.

S63.  Pearce et al., Proc. Natl. Acad. Sci. USA 98 (2001) 12843.

Isolation  from tobacco of RALF, a polypeptide hormone that arrests  root growth and development.

S64.  Verma et al., Mol. Biol. Cell 11 (2000) 3425.

Proteomics: SCX-RPC for identification of proteasomal proteins.

S65.  Davis et al., J. Chromatogr. B 752 (2001) 281.

Proteomics:  assessment of SCX-RPC- MS/MS for proteomics analyses.

S66.  Griffin et al., Anal. Chem. 73 (2001) 978

Proteomics: identification of ICAT-labelled yeast proteins via ICAT labelling  and SCX (offline)-RPC-MALDI QTOF MS.

S67.  Ideker et al., Science 292 (2001) 929.

Proteomics:  comparison of yeast protein and mRNA content changes  (ICAT used).

S68.  Koc et al., J. Biol. Chem 276 (2001) 43958.

Proteomics: identification of proteins in the large subunit of bovine mitochondrial  ribosome (ICAT used).

S69.  Peng and Gygi, J. Mass Spectrom. 36 (2001) 1083.

Proteomics: a tutorial.

S70.  Gygi et al., J. Proteome Res. (Web release date: 1/18/2002)

Proteomics of low abundance proteins: . assessment of reproducibility  and sensitivity using SCX-RPC-MS/MS and ICAT.

[Chromatographyhop] [Whats New?] [Customer Support] [Expert Training] [Networking] [LC Product Supplier] [ACE / ACT] [Hichrom] [Kromasil] [PolyLC] [Daicel] [Mitsubishi] [Agilent] [Grace Davison] [GL Science] [Merck] [Macherey-Nagel] [Perkin Elmer] [Sigma Aldrich] [Whatman] [Waters] [Thermo] [GC Product Supplier] [Workimprovment] [Equipment] [Column Technology.] [Phases] [Processes] [Contacting us] [Terms & Conditions]

The chromatographyshop web-site is Copyright protected by  LCC Engineering & Trading GmbH 1995 - 2010