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Enzymatic digestion of human plasma inter-alpha-trypsin inhibitor by snake venom metalloproteinases.
- Source :
-
Comparative biochemistry and physiology. B, Comparative biochemistry [Comp Biochem Physiol B] 1985; Vol. 80 (3), pp. 507-12. - Publication Year :
- 1985
-
Abstract
- Incubation of human plasma inter-alpha-trypsin inhibitor with crotalid, viperid, colubrid or elapid venoms resulted in random cleavage of the intact inhibitor (200,000 mol. wt) and formation of inhibitor of 130,000, 77,000, 58,000, and 38,000 mol. wt, along with several minor products. The overall patterns of digestion varied among the venoms studied. However, a 77,000 mol. wt inhibitor cleavage product was formed by all venoms tested, and this fragment was resistant to proteolysis even after a 24 hr incubation with the venoms. Venom pre-treated with phenylmethylsulfonyl fluoride digested inter-alpha-trypsin inhibitor; however, pre-treatment with EDTA completely stopped the reaction, indicating that venom metalloproteinases were responsible for the inhibitor digestion. The inhibitor cleavage products retained the ability to inhibit trypsin, but had no inhibitory activity against venom proteinases.
- Subjects :
- Crotalid Venoms metabolism
Edetic Acid pharmacology
Elapid Venoms metabolism
Humans
Hydrolysis
Metalloendopeptidases
Molecular Weight
Peptide Fragments metabolism
Snake Venoms antagonists & inhibitors
Trypsin Inhibitors metabolism
Viper Venoms metabolism
Alpha-Globulins metabolism
Endopeptidases metabolism
Snake Venoms metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0305-0491
- Volume :
- 80
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Comparative biochemistry and physiology. B, Comparative biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 2408815
- Full Text :
- https://doi.org/10.1016/0305-0491(85)90281-0