Abstract
Abstract Platelets lysed with Triton X-100 contain 3.44 +/- 1.27 (SD) microgram of fibronectin (cold-insoluble globulin) per 10(9) platelets. Fibronectin was partially released from washed whole platelets by collagen or thrombin, and its release by collagen was inhibited by aspirin. Analysis of subcellular fractions obtained by density-gradient centrifugation of disrupted platelets indicated that fibronectin was contained in the alpha granules. Fibrinogen depleted of fibronectin (less than 2 microgram/mg) supported ADP-induced aggregation as effectively as fibrinogen contaminated with this protein, thus reinforcing the generally held view that fibrinogen itself is the necessary protein cofactor in this reaction.
Dates
Type | When |
---|---|
Created | 5 years, 10 months ago (Oct. 13, 2019, 1:07 a.m.) |
Deposited | 5 years, 9 months ago (Nov. 19, 2019, 2:47 p.m.) |
Indexed | 1 year, 3 months ago (May 12, 2024, 4:01 p.m.) |
Issued | 46 years, 2 months ago (July 1, 1979) |
Published | 46 years, 2 months ago (July 1, 1979) |
Published Print | 46 years, 2 months ago (July 1, 1979) |
@article{Zucker_1979, title={Release of platelet fibronectin (cold-insoluble globulin) from alpha granules induced by thrombin or collagen; lack of requirement for plasma fibronectin in ADP-induced platelet aggregation}, volume={54}, ISSN={1528-0020}, url={http://dx.doi.org/10.1182/blood.v54.1.8.8}, DOI={10.1182/blood.v54.1.8.8}, number={1}, journal={Blood}, publisher={American Society of Hematology}, author={Zucker, MB and Mosesson, MW and Broekman, MJ and Kaplan, KL}, year={1979}, month=jul, pages={8–12} }