The IR spectra and structure of the methyl ester of dimethylphosphinic acid

The alcoholic extract of the Apocynum venentum (AV)bark were purified by silica gel column chromatography. The isolated chemical constituents were identified by MS, NMR, IR spectra. The main chemicals isolated from AV bark were quercetin (1), kaempferol (2), isoquercitrin (3), luteolin (4), hyperoside(5), 7-hydroxy-6-methoxy-2H-1-benzopyran-2-one (6), b-sitosterol (7), stigmasterol (8), 3, 4-dihydroxy-benzoic acid methyl ester (9), 3, 5-dihydroxybenzaldehyde (10) and 3, 4-dihydroxy-benzoic acid (11). The compounds (1)～(6) and (8)～(11) were obtained from AV bark for the first time.

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A last resort method for methyl ester hydrolysis using trimethyltin hydroxide under microwave conditions.

ChemSpider Synthetic Pages ◽

10.1039/sp263 ◽

2007 ◽

Author(s):

Andrew McCarroll

Keyword(s):

Methyl Ester ◽

Ester Hydrolysis

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Administration of Nω-?-Arginine Methyl Ester (L-NAME) impairs endothelium-dependent relaxation in gravid but not nongravid rats

Journal of the Society for Gynecologic Investigation ◽

10.1016/s1071-5576(02)00220-4 ◽

2003 ◽

Vol 10 (2) ◽

pp. 74-81 ◽

Cited By ~ 9

Author(s):

J Martínez-Orgado

Keyword(s):

Methyl Ester ◽

Endothelium Dependent Relaxation

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The Effect of Some Synthetic Arginyl and Lysyl Compounds on Clotting and Fibrinolysis

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649094 ◽

1972 ◽

Vol 28 (02) ◽

pp. 289-298 ◽

Cited By ~ 1

Author(s):

M. J Weinstein ◽

R. F Doolittle

Keyword(s):

Methyl Ester ◽

Thrombin Activation

SummaryThe effects of a number of synthetic arginyl- and lysyl-compounds on clotting and fibrinolysis have been studied. The lysyl derivatives had no significant effect on the clotting of recalcified plasma or recalcified euglobulin preparations, but tosyllysine (TL) and tosyllysine methyl ester (TLME) were very effective inhibitors of fibrinolysis. Certain arginyl-peptides (in particular, tosylarginylsarcosine methyl ester) were very effective at delaying clotting in these systems. These same substances gave rise to an exaggerated thrombin production, however, evidently by interfering with the natural thrombin activation of plasma antithrombin(s).

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Activity of Plasmin and Streptokinase-Activator on Substituted Arginine and Lysine Esters

Thrombosis and Haemostasis ◽

10.1055/s-0038-1655623 ◽

1966 ◽

Vol 16 (01/02) ◽

pp. 018-031 ◽

Cited By ~ 13

Author(s):

S Sherry ◽

Norma Alkjaersig ◽

A. P Fletcher

Keyword(s):

Molecular Structure ◽

Methyl Ester ◽

Comparative Studies ◽

Esterase Activity ◽

Methyl Esters ◽

Hydrolytic Activity ◽

The Other ◽

Other Hand

SummaryComparative studies have been made of the esterase activity of plasmin and the streptokinase-activator of plasminogen on a variety of substituted arginine and lysine esters. Human plasmin preparations derived by different methods of activation (spontaneous in glycerol, trypsin, streptokinase (SK) and urokinase) are similar in their esterase activity; this suggests that the molecular structure required for such esterase activity is similar for all of these human plasmins. Bovine plasmin, on the other hand, differs from human plasmin in its activity on several of the substrates studied (e.g., the methyl esters of benzoyl arginine and tosyl, acetyl and carbobenzoxy lysine), a finding which supports the view that molecular differences exist between the two animal plasmins. The streptokinase-activator hydrolyzes both arginine and lysine esters but the ratios of hydrolytic activity are distinct from those of plasmin and of other activators of plasminogen. The use of benzoyl arginine methyl ester as a substrate for the measurement of the esterase activity of the streptokinase-activator is described.

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