Affinity ligands

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Separation or purification

Reexamination Certificate

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C530S412000, C530S328000, C530S329000

Reexamination Certificate

active

08058410

ABSTRACT:
Disclosed is an affinity matrix comprising a solid phase and an affinity ligand comprising peptide bonds coupled to this solid phase, wherein the affinity ligand comprising peptide bond is selected from the following group of ligands: a) peptides comprising the formula X1X2X3X4, wherein X1to X4are amino acid residues and at least two of X1to X4is W, Y or F; b) peptides comprising the formula X5X6X7X8, wherein X5to X8are amino acid residues, at least one of X5to X8is W, and at least one of X5to X8is E or D; and c) poly-amino acids consisting of an amino acid monomer of the group consisting of R, K, E and D and an amino acid monomer of the group consisting of Y, F and W, preferably poly-KY, poly-KF, poly-KW, poly-RY, poly-RF, poly-RW, poly-EY, poly-DY, poly-EF, poly-EW, poly-DF and poly-DW, with the proviso that the peptides according to a) and b) have a maximum length of 35 amino acid residues and that the poly-amino acids according to c) have a minimum length of 20 amino acid residues.

REFERENCES:
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Alloza I et al., “Cross-linking approach to affinity capture of protein complexes from chaotrop-solubilized cell lysates”, Analytical Biochemistry, Academic Press, vol. 324, No. 1, Jan. 1, 2004, pp. 137-142.
Database NCBI [Online] 2001, Davoodi-Semiromi A et al.: “Direct submission” XP002397791, retrieved from NCBI, Database accession No. AAL05891, abstract.
Database NCBI [Online] 1999, Hongyuan J & Meiyun Z: “Direct submission” XP002397792, retrieved from NCBI, Database accession No. AAD56386, abstract.
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Davoodi-Semiromi A et al., Diabetes, vol. 51, No. 7, 2002, pp. 2334-2336., Isr.

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