leupeptins and arginine-methyl-ester

leupeptins has been researched along with arginine-methyl-ester* in 1 studies

Other Studies

1 other study(ies) available for leupeptins and arginine-methyl-ester

Article	Year
L-arginine methylester reduces Ca2+/Cl(-)-dependent L-[3H]glutamate binding and Ca2+-activated neutral protease activity in rat hippocampal membranes. Fundamental & clinical pharmacology, 1987, Volume: 1, Issue:5 Specific binding of L-[3H]glutamate was measured in Tris-HCl buffer in rat hippocampal membranes. In these experimental conditions 1 mM CaCl2 induced an increase in binding due to an increase in Bmax. L-Arginine methylester did not modify the Cl(-)-dependent binding of L-[3H]glutamate, but it decreased Ca2+/Cl(-)-stimulated binding in a dose-dependent manner, decreasing Bmax without changing KD. L-Arginine methylester reduced calcium-activated neutral protease activity in a dose-dependent manner. Serine protease inhibitors (aprotinin and di-isopropylfluorophosphate) did not affect L-[3H]glutamate binding, whereas leupeptin reduced it in a dose-dependent manner. L-Arginine did not mimic the effect of L-arginine methylester in either model. Topics: Animals; Arginine; Calcium Chloride; Enzyme Activation; Glutamates; Hippocampus; In Vitro Techniques; Leupeptins; Male; Peptide Hydrolases; Rats; Rats, Inbred Strains	1987

Article

Year

L-arginine methylester reduces Ca2+/Cl(-)-dependent L-[3H]glutamate binding and Ca2+-activated neutral protease activity in rat hippocampal membranes.

Fundamental & clinical pharmacology, 1987, Volume: 1, Issue:5

Specific binding of L-[3H]glutamate was measured in Tris-HCl buffer in rat hippocampal membranes. In these experimental conditions 1 mM CaCl2 induced an increase in binding due to an increase in Bmax. L-Arginine methylester did not modify the Cl(-)-dependent binding of L-[3H]glutamate, but it decreased Ca2+/Cl(-)-stimulated binding in a dose-dependent manner, decreasing Bmax without changing KD. L-Arginine methylester reduced calcium-activated neutral protease activity in a dose-dependent manner. Serine protease inhibitors (aprotinin and di-isopropylfluorophosphate) did not affect L-[3H]glutamate binding, whereas leupeptin reduced it in a dose-dependent manner. L-Arginine did not mimic the effect of L-arginine methylester in either model.

Topics: Animals; Arginine; Calcium Chloride; Enzyme Activation; Glutamates; Hippocampus; In Vitro Techniques; Leupeptins; Male; Peptide Hydrolases; Rats; Rats, Inbred Strains

1987