Abstract
Adhesiveness in citrated whole blood is critically pH dependent at hydrogen ion concentrations close to the physiological range. While platelets in platelet-rich plasma (PRP) adhere poorly in glass-bead columns, washed platelets and particularly gel-filtered platelets (GFP), prepared from PRP, are adhesive. Separation of PRP on a Sepharose 2B column revealed the presence of an inhibitor of adhesiveness of GFP. The inhibitory compound is thermostable and nondialyzable. It is inactivated completely by pronase digestion and partially by trypsin digestion. It is distinct from any one of the known platelet factors. Washed erythrocytes and erythrocyte membranes attenuate the potency of the inhibitor. Following separation by isoelectric focusing, the inhibitory activity is limited primarily to a single fraction with an isoelectric point of 5.1 containing equal amounts of proteins and lipids. Two protein bands are revealed by sodium dodecyl sulfate-gel electrophoresis of the purified fraction. It is concluded that PRP contains a compound, apparently a lipoprotein, which inhibits platelet adhesiveness.
| Original language | English |
|---|---|
| Pages (from-to) | 264-271 |
| Number of pages | 8 |
| Journal | Israel Journal of Medical Sciences |
| Volume | 13 |
| Issue number | 3 |
| State | Published - 1 Jan 1977 |
ASJC Scopus subject areas
- Bioengineering