Abstract
Screening of the biochemical-pharmacological properties of the crude venom from the snake Lachesis muta indicated the presence of phospholipase A2 (PLA2; 5260 U/mg protein), procoagulant (2630 U/mg protein), platelet aggregating (43 U/mg protein) and caseinolytic activities (6670 U/mg protein). These activities were separated by filtration of the crude venom on Sephacryl S-200. The material containing PLA2 activity was further fractioned by DEAE-cellulose ion exchange chromatography into four active fractions (F-I to F-IV, containing 1.7, 1.2, 0.3, and 0.05% of the crude venom protein, respectively) by stepwise elution with buffers of increasing ionic strength. All fractions presented a molecular weight of approximately 15,000 and isoelectric points in the range pH 4.6-6.0. In addition to their indirect hemolytic activity, the partially purified fractions inhibited platelet aggregation induced either by collagen or thrombin. p-Bromophenacyl bromide-treated fractions lost both phospholipase A2 activity and their inhibitory effect on collagen-induced platelet aggregation.
Original language | English (US) |
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Pages (from-to) | 459-463 |
Number of pages | 5 |
Journal | Brazilian Journal of Medical and Biological Research |
Volume | 26 |
Issue number | 5 |
State | Published - May 1993 |
Externally published | Yes |
ASJC Scopus subject areas
- Biophysics
- Neuroscience(all)
- Biochemistry
- Physiology
- Immunology
- Pharmacology, Toxicology and Pharmaceutics(all)
- Cell Biology