Purification and partial characterization of a bioactive substance from rat's vessel wall independent of prostacyclin production

A. C. Kempfer, N. Maugeri, C. Farias, E. Bermejo, M. Gimeno, J. P. Frontroth, M. Lazzari

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish
Pages (from-to)127-135
Number of pages9
JournalThrombosis Research
Volume52
Issue number2
DOIs
Publication statusPublished - Oct 15 1988

Keywords

  • antiaggregatory vascular protein

ASJC Scopus subject areas

  • Cardiology and Cardiovascular Medicine
  • Hematology

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