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casein + H2O
hydrolyzed casein
-
endopeptidase
-
?
collagen I + H2O
?
-
-
-
-
?
Collagen IV + H2O
?
-
-
-
-
?
collagen VI + H2O
?
-
from human placenta
-
-
?
fibrinonectin + H2O
?
-
from human plasma
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
cleavage of His5-Leu, His10-Leu, Ala14-Leu, Tyr16-Leu and Phe24-Phe
-
?
Matrigel + H2O
?
-
-
-
-
?
type I collagen
?
-
-
-
-
?
Vitronectin + H2O
?
-
from human plasma
-
-
?
von Willebrand factor + H2O
?
-
-
-
-
?
additional information
?
-
casein + H2O
?
-
enzyme stabilized by CaCl2
-
-
?
Fibrin + H2O
?
-
-
-
-
?
Fibrin + H2O
?
the enzyme specifically cleaves the alpha-polymer and alpha-chain of the fibrin molecule, in contrast gamma-gamma dimer and beta-chain of the fibrin are found to be resistant to the enzyme
-
-
?
Fibrinogen + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
identification of peptides generated by bothropasin proteolytic activity. Among the fibrinogen derived peptides identified by mass spectrometry, analogous of endogenous products like the fibrinopeptides A and B are found, as well as other sequences described in the literature with vasoactive or antiangiogenic properties
-
-
?
Fibrinogen + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
identification of peptides generated by bothropasin proteolytic activity. For most of the peptides no biological activity is described. Exceptionally a peptide that is known as a bond site for B cells is found
-
-
?
Fibronectin + H2O
?
-
-
-
?
additional information
?
-
comparison of hemorrhagic, caseinolytic and fibrinogenolytic activities of metalloproteinases HF3, bothropasin, the DC protein and metalloproteinase BJ-PI. Hemorrhagic activity of bothropasin is 0.006 mg to produce a hemorrhagic area of 1 cm2. Fibrinogenolytic activity of bothropasin is 9.8 units/mg
-
-
?
additional information
?
-
-
comparison of hemorrhagic, caseinolytic and fibrinogenolytic activities of metalloproteinases HF3, bothropasin, the DC protein and metalloproteinase BJ-PI. Hemorrhagic activity of bothropasin is 0.006 mg to produce a hemorrhagic area of 1 cm2. Fibrinogenolytic activity of bothropasin is 9.8 units/mg
-
-
?
additional information
?
-
-
bothropasin degradation profiles of fibrinogen, fibronectin, vitronectin, von Willebrand factor, collagens IV and VI, laminin and Matrigel in comparison to the other three snake venom metalloproteinases of Bothrops jararaca, binding to plasma and extracellular matrix proteins, overview. Collagen I is degraded only by bothropasin
-
-
?
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Hyperalgesia
Jararhagin, a snake venom metalloproteinase, induces mechanical hyperalgesia in mice with the neuroinflammatory contribution of spinal cord microglia and astrocytes.
Myotoxicity
Effect of monospecific antibodies against baltergin in myotoxicity induced by Bothrops alternatus venom from northeast of Argentina. Role of metalloproteinases in muscle damage.
Myotoxicity
Inhibition of the myotoxic and hemorrhagic activities of crotalid venoms by Eclipta prostrata (Asteraceae) extracts and constituents.
Neoplasm Metastasis
Recombinant snake venom metalloproteinase inhibitor BJ46A inhibits invasion and metastasis of B16F10 and MHCC97H cells through reductions of matrix metalloproteinases 2 and 9 activities.
Osteosarcoma
Differential susceptibility of osteosarcoma cells and primary osteoblasts to cell detachment caused by snake venom metalloproteinase protein.
Pancreatitis
A novel recombinant snake venom metalloproteinase from Agkistrodon acutus protects against taurocholate-induced severe acute pancreatitis in rats.
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additional information
-
role of the non-catalytic domains of snake venom metalloproteinases, interaction of four snake venom metalloproteinases of different domain compositions and glycosylation levels, from Bothrops jararaca venom, with plasma and extracellular matrix proteins, overview
physiological function
-
haemorrhagic effect of bothropasin on mouse skin, overview
physiological function
in the enzyme-treated mouse skin there is evidence of degradation of extracellular matrix (collagens and proteoglycans), cytosolic, cytoskeleton, and plasma protein as well as activation of collagenase
physiological function
beyond to the degradation of human proteins, bothropasin can generate bioactive peptides, which may participate in the envenoming process by Bothrops snakes
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Mandelbaum, F.R.; Reichel, A.P.; Assakura, M.T.
Isolation and characterization of a proteolytic enzyme from the venom of the snake Bothrops jararaca (Jararaca)
Toxicon
20
955-972
1982
Bothrops jararaca
brenda
Mandelbaum, F.R.; Assakura, M.T.; Reichl, A.P.; Serrano, S.M.
Bothropasin
Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
658-659
2004
Bothrops jararaca
-
brenda
Carneiro, S.M.; Zablith, M.B.; Kerchove, C.M.; Moura-da-Silva, A.M.; Quissell, D.O.; Markus, R.P.; Yamanouye, N.
Venom production in long-term primary culture of secretory cells of the Bothrops jararaca venom gland
Toxicon
47
87-94
2006
Bothrops jararaca
brenda
Muniz, J.R.; Ambrosio, A.L.; Selistre-de-Araujo, H.S.; Cominetti, M.R.; Moura-da-Silva, A.M.; Oliva, G.; Garratt, R.C.; Souza, D.H.
The three-dimensional structure of bothropasin, the main hemorrhagic factor from Bothrops jararaca venom: insights for a new classification of snake venom metalloprotease subgroups
Toxicon
52
807-816
2008
Bothrops jararaca (O93523), Bothrops jararaca
brenda
Oliveira, A.K.; Paes Leme, A.F.; Assakura, M.T.; Menezes, M.C.; Zelanis, A.; Tashima, A.K.; Lopes-Ferreira, M.; Lima, C.; Camargo, A.C.; Fox, J.W.; Serrano, S.M.
Simplified procedures for the isolation of HF3, bothropasin, disintegrin-like/cysteine-rich protein and a novel P-I metalloproteinase from Bothrops jararaca venom
Toxicon
53
797-801
2009
Bothrops jararaca (O93523), Bothrops jararaca
brenda
Oliveira, A.K.; Paes Leme, A.F.; Asega, A.F.; Camargo, A.C.; Fox, J.W.; Serrano, S.M.
New insights into the structural elements involved in the skin haemorrhage induced by snake venom metalloproteinases
Thromb. Haemost.
104
485-497
2010
Bothrops jararaca
brenda
Paes Leme, A.; Sherman, N.; Smalley, D.; Sizukusa, L.; Oliveira, A.; Menezes, M.; Fox, J.; Serrano, S.
Hemorrhagic activity of HF3, a snake venom metalloproteinase: Insights from the proteomic analysis of mouse skin and blood plasma
J. Proteome Res.
11
279-291
2012
Bothrops jararaca (Q98UF9), Bothrops jararaca
brenda
Srinivasa, V.; Sundaram, M.; Anusha, S.; Hemshekhar, M.; Nayaka, S.; Kemparaju, K.; Basapp, B.; Girish, K.; Rangappa, K.
Novel apigenin based small molecule that targets snake venom metalloproteases
PLoS ONE
9
e106364
2014
Echis carinatus (Q9PRP9), Echis carinatus
brenda
Silva, C.C.F.; Menezes, M.C.; Palomino, M.; Oliveira, A.K.; Iwai, L.K.; Faria, M.; Portaro, F.V.
Peptides derived from plasma proteins released by bothropasin, ametalloprotease present in the Bothrops jararaca venom
Toxicon
137
65-72
2017
Bothrops jararaca (O93523), Bothrops jararaca
brenda