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Primary structure of the heparin-binding site of type V collagen
- Source :
- Biochimica et biophysica acta. 1035(2)
- Publication Year :
- 1990
-
Abstract
- The abilities of collagens, type I, II, III, IV, and V, to bind heparin were examined by heparin-affinity chromatography and binding studies with [35S]heparin. At a physiological pH and ionic strength, only type V collagen bound to heparin. Collagens type I and II showed higher affinities than types III and IV for heparin, but did not bind to a heparin column at a physiological ionic strength. The heparin binding site of type V collagen was located in a 30 kDa CNBr fragment of the alpha 1(V) chain, and the amino acid sequence of this fragment was determined. The 30 kDa fragment contained a cluster of basic amino acid residues, and enzymatic cleavage within this basic domain greatly reduced the heparin-binding activities of the resulting peptides. Thus this basic region is probably the heparin-binding site of type V collagen.
- Subjects :
- Stereochemistry
Molecular Sequence Data
Biophysics
Cleavage (embryo)
Biochemistry
Peptide Mapping
Chromatography, Affinity
Affinity chromatography
medicine
Animals
Humans
Amino Acid Sequence
Binding site
Molecular Biology
Peptide sequence
Chromatography, High Pressure Liquid
chemistry.chemical_classification
Binding Sites
Chemistry
Heparin
Protein primary structure
Peptide Fragments
Enzyme
Ionic strength
Cattle
Collagen
medicine.drug
Peptide Hydrolases
Subjects
Details
- ISSN :
- 00063002
- Volume :
- 1035
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Biochimica et biophysica acta
- Accession number :
- edsair.doi.dedup.....1c8b5df2576c71d665930ab7ca28cd14