Human serum amyloid P component binds to a specific peptide in the presence of calcium.
Human serum amyloid P component (SAP) binds to a carboxyl-terminal peptide of residues 160-204 of SAP itself in the presence of calcium. A set of sequentially overlapping decapeptides covering the entire length of residues 160-204 of SAP was synthesized on polyethylene pins to be used for binding assay, and six overlapping peptides in residues 190-204 (Tyr-Glu-Ile-Arg-Gly-Tyr-Val-Ile-Ile-Lys-Pro-Leu-Val-Trp-Val) were found to have equally high affinity for SAP. The validity of using peptides on polyethylene pins was shown by the binding assay using 11-residue soluble peptide corresponding to residues 194-204. Replacement of the Lys or the Ile residues with Glu abolished the binding activity.
Hamazaki
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Department of Biology, Kitasato University School of Medicine, Kanagawa, Japan.
D000595:Amino Acid Sequence; D002118:Calcium / Q000494:pharmacology*; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism; D000685:Serum Amyloid A Protein / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D014357:Trypsin
D009842:Oligopeptides; D010446:Peptide Fragments; D000685:Serum Amyloid A Protein; D014357:Trypsin; D002118:Calcium