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scopus(3)
Biological and biochemical characterization of new basic phospholipase A<inf>2</inf> BmTX-I isolated from Bothrops moojeni snake venom
ArticleAbstract: BmTX-I, an Asp49 phospholipase A2, was purified from Bothrops moojeni venom after only one chromatogPalabras claves:Asp49 phospholipase A2, characterization, Edema-forming activity, Myonecrosis and interleukin-6 response, Neuromuscular blockade, Snake venomAutores:Baldasso P.A., Calgarotto A.K., Damico D.C.S., Eberlin M.N., Marangoni S., Ponce-Soto L.A., Saulo L. Silva, Souza G.H.M.F.Fuentes:scopusMolecular modeling and inhibition of phospholipase A<inf>2</inf> by polyhydroxy phenolic compounds
ArticleAbstract: Phospholipases A2 are enzymes responsible for the hydrolysis of membrane phospholipids that releasePalabras claves:DFT, Enzymatic kinetics, molecular modeling, PHENOLIC COMPOUNDS, PLA 2Autores:Baldasso P.A., Calgarotto A.K., Comar M., Damico D.C.S., Marangoni S., Maso V., Oliveira A.R.M., Oliveira K.M.T., Saulo L. Silva, Veber C.L., Villar J.A.F.P.Fuentes:scopusLmrTX, a basic PLA<inf>2</inf> (D49) purified from Lachesis muta rhombeata snake venom with enzymatic-related antithrombotic and anticoagulant activity
ArticleAbstract: A basic phospholipase A2 (LmrTX) isoform was isolated from Lachesis muta rhombeata snake venom and pPalabras claves:Anticoagulant activity, Arterial thrombosis, Lachesis muta rhombeata venom, Phospholipase A 2, Photochemical injury, Platelet aggregationAutores:Antunes E., Damico D.C.S., de Souza R.C.G., Marangoni S., Mendes C.B., Nery-Diez A.C.C., Saulo L. Silva, Torres-Huaco F.D., Vassequi-Silva T., Vicente C.P., Werneck C.C.Fuentes:scopus