Primary structure of a protein isolated from reef shark(Carcharhinus springeri)cartilage that is similar to the mammalian C-type lectin homolog, tetranectin
Author:
Funder
North America and NIH
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.5560010116/fullpdf
Reference13 articles.
1. The effect of link protein on proteoglycan aggregate structure. An electron microscopic study of the molecular architecture and dimensions of proteoglycan aggregates reassembled from the proteoglycan monomers and link proteins of bovine fetal epiphyseal cartilage;Buckwalter;J. Biol. Chem.,1984
2. Interaction of tetranectin with sulfated polysaccharides and trypan blue;Clemmensen;Scand. J. Clin. Lab. Invest.,1989
3. A tetranectin-related protein is produced and deposited in extracellular matrix by human embryonal fibroblasts;Clemmensen;Eur. J. Biochem.,1991
4. Purification and characterization of a novel, oligomeric, plasminogen kringle 4 binding protein from human plasma: Tetranectin;Clemmensen;Eur. J. Biochem.,1986
5. Complete coding sequence and deduced primary structure of the human cartilage large aggregating proteoglycan, aggrecan;Doege;J. Biol. Chem.,1991
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