A promising methyl ester of pectic acid polysaccharide in biomedicine and pharmaceutics applications: Oxidation of methyl ester of pectic acid by alkaline hexacyanoferrate(III). A kinetic and mechanistic orientation

2019 ◽  
Vol 51 (7) ◽  
pp. 484-496
Author(s):  
Refat Hassan ◽  
Samia Ibrahim
Author(s):  
George F. Leeper

Polysaccharide elementary fibrils are usually fasciated into microfibrils of from one hundred to a few hundred Angstroms wide. Cellulose microfibrils when subjected to acid treatment dissociate into component elementary fibrils. For pectic acid it was observed that variations in pH could cause a change in the fasciation of the elementary fibrils.Solutions of purified pectic acid and sodium phosphotungtate were adjusted to various pH levels with NaOH or HCl and diluted to give a final concentration of 0.5 and 1% for the polysaccharide and negative stains respectively. Micrographs were made of the samples after drying on a carbon film covered grid. The average number of elementary fibrils was determined by counting the number of elementary fibrils in each fascicle intersected by lines drawn across the micrograph.


1972 ◽  
Vol 28 (02) ◽  
pp. 289-298 ◽  
Author(s):  
M. J Weinstein ◽  
R. F Doolittle

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).


1966 ◽  
Vol 16 (01/02) ◽  
pp. 018-031 ◽  
Author(s):  
S Sherry ◽  
Norma Alkjaersig ◽  
A. P Fletcher

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.


2002 ◽  
Vol 76 (3) ◽  
pp. 252 ◽  
Author(s):  
Alessandra Belvedere ◽  
Francisco Boscá ◽  
M. Consuelo Cuquerella ◽  
Guido de Guidi ◽  
Miguel A. Miranda

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