[CITATION][C] [4] Thrombospondins
P Bornstein, EH Sage - Methods in Enzymology, 1994 - Elsevier
The characterization of platelet thrombospondin (TSP), its electron microscopic appearance,
and its subcellular location were first described by Lawler and co-workers in 1978.1
However, TSP had been identified earlier as a thrombin-sensitive protein that was released
on activation of human platelets. 2'3 Thrombospondin is a disulfide-bonded trimer of three
identical chains with a monomer molecular mass of about 140,000 Da. The predicted amino
acid composition of human TSP1, based on analyses of DNA clones, 4'5 provides for a …
and its subcellular location were first described by Lawler and co-workers in 1978.1
However, TSP had been identified earlier as a thrombin-sensitive protein that was released
on activation of human platelets. 2'3 Thrombospondin is a disulfide-bonded trimer of three
identical chains with a monomer molecular mass of about 140,000 Da. The predicted amino
acid composition of human TSP1, based on analyses of DNA clones, 4'5 provides for a …