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Autocatalytic acylation of phospholipase-like myotoxins
(1995-04)
Several snake venoms contain a phospholipase A2 in which position 49 in the active site is occupied by a lysine or a serine instead of the aspartate residue normally found. Although these proteins do not bind Ca2+ and are ...
Effects of Bothrops asper (terciopelo) myotoxin III, a basic phospholipase A2, on liposomes and mouse gastrocnemius muscle
(1993-02)
The action of Bothrops asper myotoxin III, a basic phospholipase A2 which induces acute muscle damage, was studied in mouse gastrocnemius muscle in vivo and in vitro and in multilamellar liposomes. Myonecrosis occurred ...
Autocatalytic acylation of phospholipase-like myotoxins
(1995-04)
Several snake venoms contain a phospholipase A2 in which position 49 in the active site is occupied by a lysine or a serine instead of the aspartate residue normally found. Although these proteins do not bind Ca2+ and are ...
Effects of Bothrops asper (terciopelo) myotoxin III, a basic phospholipase A2, on liposomes and mouse gastrocnemius muscle
(1993-02)
The action of Bothrops asper myotoxin III, a basic phospholipase A2 which induces acute muscle damage, was studied in mouse gastrocnemius muscle in vivo and in vitro and in multilamellar liposomes. Myonecrosis occurred ...
Neutralization of myotoxic phospholipases A2 from the venom of the snake Bothrops asper by monoclonal antibodies
(1992)
The neutralization of two myotoxic phospholipases A2 from the venom of Bothrops asper, myotoxins I and II, by two murine monoclonal antibodies is reported. The monoclonal antibodies, MAb-3 and Mab-4, recognize different ...
The amino acid sequence of a myotoxic phospholipase from the venom of Bothrops asper
(1990)
A myotoxic, basic phospholipase A2 (pI greater than 9.5) with anticoagulant activity has been purified from the venom of Bothrops asper, and its amino acid sequence determined by automated Edman degradation. It is distinct ...
The amino acid sequence of a myotoxic phospholipase from the venom of Bothrops asper
(1990)
A myotoxic, basic phospholipase A2 (pI greater than 9.5) with anticoagulant activity has been purified from the venom of Bothrops asper, and its amino acid sequence determined by automated Edman degradation. It is distinct ...
Insights into metal ion binding in phospholipases A(2): ultra high-resolution crystal structures of an acidic phospholipase A(2) in the Ca2+ free and bound states
(Elsevier B.V., 2006-05-01)
The electrophile Ca2+ is an essential multifunctional co-factor in the phospholipase A(2) mediated hydrolysis of phospholipids. Crystal structures of an acidic phospholipase A(2) from the venom of Bothrops jararacussu have ...
Snake venom phospholipase A(2) inhibitors: Medicinal chemistry and therapeutic potential
(Bentham Science Publ Ltd, 2007-01-01)
Phospholipases A(2) (PLA(2)s) are commonly found in snake venoms from Viperidae, Hydrophidae and Elaphidae families and have been extensively studied due to their pharmacological and physiopathological effects in living ...
Snake venom phospholipase A(2) inhibitors: Medicinal chemistry and therapeutic potential
(Bentham Science Publ Ltd, 2007-01-01)
Phospholipases A(2) (PLA(2)s) are commonly found in snake venoms from Viperidae, Hydrophidae and Elaphidae families and have been extensively studied due to their pharmacological and physiopathological effects in living ...