PMID: 8599184Oct 1, 1995Paper

Purification and characterization of three alpha 2-antiplasmin and alpha 2-macroglobulin inactivating enzymes from the venom of the Mexican west coast rattlesnake (Crotalus basiliscus)

Toxicon : Official Journal of the International Society on Toxinology
P SvobodaT A Freyvogel

Abstract

Three distinct alpha 2PI (alpha 2-antiplasmin) degrading and alpha 2M (alpha 2-macroglobulin) inhibiting enzymes, named proteinase a, b and c, have been purified from the venom of Crotalus basiliscus (the Mexican west coast rattlesnake) by fast protein liquid chromatography (anion-exchange chromatography and gel filtration chromatography). SDS-PAGE revealed that proteinase a and b had similar mol. wts (approximately 23,500), whereas proteinase c displayed a mol.wt of approximately 24,200. Their isoelectric points were found to be acidic, ranging from pH 4.8 to 5.7. The proteinase activity of all three enzymes was inhibited in the presence of EDTA. Dependent on enzyme concentration, a progressive and catalytic inactivation of alpha 2PI was induced, leading to an almost complete loss of the plasmin inhibitory activity at a molar ratio of enzyme: alpha 2PI = 0.1 within 60 min. The ability of alpha 2M to protect the esterolytic activity of trypsin from inhibition by soybean trypsin inhibitor was only reduced at a molar ratio of enzyme: alpha 2M = 0.5, whereas no inactivation could be observed when the three venom proteinases were incubated with an excess of alpha 2M, suggesting that the inactivation occurred by complex formation bu...Continue Reading

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Citations

Dec 5, 1998·Toxicon : Official Journal of the International Society on Toxinology·F S Markland
Nov 18, 2015·Blood Coagulation & Fibrinolysis : an International Journal in Haemostasis and Thrombosis·Vance G NielsenDaniel T Redford
Mar 5, 1999·Critical Reviews in Toxicology·R HatiK K Bhattacharyya
Aug 13, 2021·Seminars in Thrombosis and Hemostasis·Gary William Moore

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