The bioactive substance from rat's vessel wall was purified by Sephadex G-75 gel filtration and by a combination of DEAE Cellulose ion exchange and Sephadex G-50 gel filtration chromatographies. Purifications of 12.5 fold and 70 fold over the initial material were achieved. PAGE of the purified material resulted in a single major band with a molecular weight estimated at 55kd-65kd. Trypsin (0.3 mg/ml) and chymotrypsin (30 mg/ml) abolished platelet antiaggregating activity. Neuraminidase (1.2 units) had no effect on platelet antiaggregating activity. This is the report of purification of aortic vessel wall antiaggregating activity independent of prostacyclin production.
- antiaggregatory vascular protein
ASJC Scopus subject areas
- Cardiology and Cardiovascular Medicine