Primary structure of human plasma fibronectin — Characterization of the 6,000 dalton C-terminal fragment containing the interchain disulfide bridges
| Autor: | Blas Frangione, Angeles Garcia-Pardo, Edward Pearlstein |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
Chemical Phenomena
Dimer Size-exclusion chromatography Biophysics Biochemistry chemistry.chemical_compound Complementary DNA Humans Amino Acid Sequence Disulfides Amino Acids Molecular Biology Peptide sequence chemistry.chemical_classification biology Chemistry Protein primary structure Cell Biology Peptide Fragments Fibronectins Amino acid Molecular Weight Fibronectin Sephadex Chromatography Gel biology.protein |
| Zdroj: | Biochemical and Biophysical Research Communications. 120:1015-1021 |
| ISSN: | 0006-291X |
| Popis: | The carboxy terminal fragment of human plasma fibronectin has been isolated after tryptic digestion and separation by DEAE-cellulose chromatography and gel filtration on Sephadex G-50. It has a molecular weight of 6,000 which changes to 3,000 after reduction indicating that the fragment is a dimer. We have determined the amino acid sequence of the 6kDa fragment and showed that it contains 26 residues including two half-cystines which form two interchain disulfide bridges. The 6kDa fragment is not phosphorylated as in bovine fibronectin although its amino acid sequence is identical to that reported for bovine plasma fibronectin. When compared to the sequence deduced from a rat cDNA, one amino acid substitution can be found. It appears that the carboxyl end of fibronectin is highly conserved among species. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|