Literature summary for 3.1.1.4 extracted from

Dias, E.H.V.; Dos Santos Paschoal, T.; da Silva, A.P.; da Cunha Pereira, D.F.; de Sousa Simamoto, B.B.; Matias, M.S.; Santiago, F.M.; Rosa, J.C.; Soares, A.; Santos-Filho, N.A.; de Oliveira, F.; Mamede, C.C.N.
BaltPLA2 A new phospholipase A2 from Bothrops alternatus snake venom with antiplatelet aggregation activity (2018), Protein Pept. Lett., 25, 943-952 .

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Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
14075	-	MALDI TOF/TOF	Bothrops alternatus
17000	-	SDS-PAGE	Bothrops alternatus

Organism

Organism	UniProt	Comment	Textmining
Bothrops alternatus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Bothrops alternatus

Source Tissue

Source Tissue	Comment	Organism	Textmining
venom	-	Bothrops alternatus	-

Subunits

Subunits	Comment	Organism
?	x * 17000, SDS-PAGE	Bothrops alternatus

Synonyms

Synonyms	Comment	Organism
BaltPLA2	-	Bothrops alternatus

pI Value

Organism	Comment	pI Value Maximum	pI Value
Bothrops alternatus	-	-	4.4

General Information

General Information	Comment	Organism
additional information	the enzyme displayed an anticoagulant action, inhibition of platelet aggregation induced by epinephrine (about 80%) and ADP (24%). The enzyme induces myonecrosis and the release of cytokines (IL-10, IL-12 and TNF-alpha) in macrophages culture	Bothrops alternatus

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Release 2023.1 (January 2023)