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Human serum amyloid P component binds to a specific peptide in the presence of calcium.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1994 Dec 15; Vol. 205 (2), pp. 1172-8. - Publication Year :
- 1994
-
Abstract
- 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.
- Subjects :
- Amino Acid Sequence
Chromatography, Gel
Chromatography, High Pressure Liquid
Humans
Hydrolysis
Molecular Sequence Data
Oligopeptides chemical synthesis
Oligopeptides metabolism
Peptide Fragments metabolism
Serum Amyloid A Protein isolation & purification
Serum Amyloid A Protein metabolism
Trypsin
Calcium pharmacology
Oligopeptides chemistry
Peptide Fragments chemistry
Serum Amyloid A Protein chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 205
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 7802647
- Full Text :
- https://doi.org/10.1006/bbrc.1994.2789