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Purification and characterization of a non-hemorrhagic metalloprotease from Agkistrodon halys brevicaudus venom
- Source :
- Biochimica et biophysica acta. 1243(1)
- Publication Year :
- 1995
-
Abstract
- A non-hemorrhagic metalloprotease (protease L4) was purified from the venom of Chinese Mamushi ( Agkistrodon halys brevicaudus ) by gel filtration and anion-exchange chromatography. Protease L4 has the molecular weight of 22 000 and its optimum pH was 8.5. The protein was stable in the pH range of 5–9 and below 40°C. The proteolytic activity was inhibited by metal-chelating agents and some metal ions. Calcium ion activated the activity dose-dependently, but had only a minor effect on the thermal and pH stability. L4 showed fibrinogenase activity, hydrolyzing only the A a chain of fibrinogen. The protease cleaved preferentially at the N-terminal of Leu and His residues of some peptides.
- Subjects :
- medicine.medical_treatment
Metal ions in aqueous solution
Size-exclusion chromatography
Molecular Sequence Data
Biophysics
chemistry.chemical_element
Venom
Hemorrhage
Mice, Inbred Strains
Viper Venoms
Calcium
Fibrinogen
Biochemistry
Substrate Specificity
Mice
Cations
Enzyme Stability
medicine
Animals
Amino Acid Sequence
Amino Acids
Molecular Biology
Chelating Agents
Metalloproteinase
Chromatography
Fibrin
Protease
Chemistry
Hydrolysis
Metalloendopeptidases
Snake venom
Agkistrodon
medicine.drug
Subjects
Details
- ISSN :
- 00063002
- Volume :
- 1243
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Biochimica et biophysica acta
- Accession number :
- edsair.doi.dedup.....e68effe3b1f0aac3ceb7b0cae461880c