PMID: 3753680Jan 2, 1986Paper

Purification and complete primary structures of the heparin-, cell-, and DNA-binding domains of bovine plasma fibronectin

European Journal of Biochemistry
K SkorstengaardS Magnusson

Abstract

The complete amino acid sequences of the heparin-, cell- and DNA-binding domains of bovine plasma fibronectin have been determined. The fragments were generated from the 170-kDa central plasmic fragment by extensive digestion with chymotrypsin, and they contain 268, 300 and 269 amino acid residues, respectively. No half-cystines or cysteines were found in these sequences. A glucosamine-based oligosaccharide group is attached to Asn-108 in the sequence of the DNA-binding domain. Only one of the three types of internal homology found in fibronectin [Petersen et al. (1983) Proc. Natl Acad. Sci. USA 80, 137-141], namely the type III homology, occurs in these three fragments, and each of them consists of approximately three stretches of this type III homology. Part of the arrangement of peptides was derived by comparison with the partial cDNA sequence for human fibronectin recently reported [Kornblihtt et al. (1984) Nucleic Acids Res. 12, 5853-5868].

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Citations

Jun 22, 2011·Proceedings of the National Academy of Sciences of the United States of America·Mary O'Connell MotherwayDouwe van Sinderen
Jun 1, 1987·The Journal of Cell Biology·G SchmidtH Kresse
Jul 30, 2002·Omics : a Journal of Integrative Biology·Ida BiunnoMonica Cattaneo
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May 7, 2009·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Immaculada MargaritGuido Grandi
Nov 30, 2019·Cells·Pietro SpezialeGiampiero Pietrocola
Dec 1, 1986·European Journal of Biochemistry·K SkorstengaardS Magnusson
Apr 24, 2021·Signal Transduction and Targeted Therapy·Jiacheng HuangYiting Qiao
Nov 20, 1987·Biochimica Et Biophysica Acta·S KubomuraH Hirano
Jan 1, 1987·Bio Systems·S K Holland, C C Blake

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