Kinetics of substitution of aquo ligands fromcis-diaquo-bis-(biguanide) cobalt(III) and chromium(III) ions by aspartic acid in ethanol?water mixtures

1989 ◽  
Vol 14 (4) ◽  
pp. 241-247 ◽  
Author(s):  
Ashis Kumar Gangopadhyay ◽  
Gauri Sankar De
Keyword(s):  
Aspartic Acid ◽  
Kinetics Of

Kinetics of the Thermal Disappearance of Radicals Formed During the Radiolysis of Aspartic Acid

2009 ◽  
Vol 59 (12) ◽  
Author(s):  
Mihai Contineanu ◽  
iulia Contineanu ◽  
Ana Neacsu ◽  
Stefan Perisanu
Keyword(s):  
Thermal Resistance ◽  
Aspartic Acid ◽  
Room Temperature ◽  
Esr Spectra ◽  
Complex Mechanism ◽  
Radical Species ◽  
Mechanisms Of Formation ◽  
Kinetics Of

The radiolysis of the isomers L-, D- and DL- of the aspartic acid, in solid polycrystalline state, was investigated at room temperature. The analysis of their ESR spectra indicated the formation of at least two radicalic entities. The radical, identified as R3, resulting from the deamination of the acid, exhibits the highest concentration and thermal resistance. Possible mechanisms of formation of three radical species are suggested, based also on literature data. The kinetics of the disappearance of radical R3 indicated a complex mechanism. Three possible variants were suggested for this mechanism.

Solid-phase polycondensation of aspartic acid 1. Kinetics of the process as evidenced by TGA and DSC data

2010 ◽  
Vol 59 (4) ◽  
pp. 806-811 ◽  
Author(s):  
V. M. Gol’dberg ◽  
S. M. Lomakin ◽  
A. V. Todinova ◽  
A. N. Shchegolikhin ◽  
S. D. Varfolomeev
Keyword(s):  
Aspartic Acid ◽  
Solid Phase ◽  
Kinetics Of ◽  
Tga And Dsc

The hydrothermal reaction kinetics of aspartic acid

2007 ◽  
Vol 71 (4) ◽  
pp. 797-820 ◽  
Author(s):  
Jenny S. Cox ◽  
Terry M. Seward
Keyword(s):  
Reaction Kinetics ◽  
Aspartic Acid ◽  
Hydrothermal Reaction ◽  
Kinetics Of

scholarly journals STUDIES OF THE EFFECT OF DIETARY PROTEIN AND CALORIC LEVELS ON THE KINETICS OF NITROGEN METABOLISM USING N15 L-ASPARTIC ACID

1959 ◽  
Vol 38 (6) ◽  
pp. 892-901 ◽  
Author(s):  
Donald P. Tschudy ◽  
Habeeb Bacchus ◽  
Sherman Weissman ◽  
Donald M. Watkin ◽  
Marjoria Eubanks ◽  
...  
Keyword(s):  
Nitrogen Metabolism ◽  
Aspartic Acid ◽  
Dietary Protein ◽  
Kinetics Of

Effect of aspartic acid on the crystallization kinetics of ACP and dentin remineralization

2021 ◽  
Vol 115 ◽  
pp. 104226
Author(s):  
Luyi Zhao ◽  
Jian Sun ◽  
Ce Zhang ◽  
Chaoqun Chen ◽  
Yi Chen ◽  
...  
Keyword(s):  
Aspartic Acid ◽  
Crystallization Kinetics ◽  
Kinetics Of

Kinetics of Oxidative Decarboxylation of DL-Aspartic acid by Potassium Permanganate

1980 ◽  
Vol 261O (1) ◽  
Author(s):  
Suresh C. Ameta ◽  
H. L. Gupta ◽  
P. N. Pande ◽  
H. C. Chaudhary
Keyword(s):  
Aspartic Acid ◽  
Potassium Permanganate ◽  
Oxidative Decarboxylation ◽  
Kinetics Of

Kinetics of solid phase thermal polycondensation of aspartic acid in evacuated system

2013 ◽  
Vol 83 (11) ◽  
pp. 2046-2049 ◽  
Author(s):  
V. A. Yablokov ◽  
Ya. A. Vasina ◽  
I. D. Grishin
Keyword(s):  
Aspartic Acid ◽  
Solid Phase ◽  
Thermal Polycondensation ◽  
Kinetics Of

scholarly journals Evidence for a two-state transition in papain that may have no close analogue in ficin. Differences in the disposition of cationic sites and hydrophobic binding areas in the active centres of papain and ficin

1980 ◽  
Vol 191 (3) ◽  
pp. 707-718 ◽  
Author(s):  
K Brocklehurst ◽  
J P G Malthouse
Keyword(s):  
Aspartic Acid ◽  
Catalytic Mechanism ◽  
Striking Difference ◽  
Compound I ◽  
Active Centre ◽  
Aspartic Acid Residue ◽  
Wide Range ◽  
Cationic Site ◽  
Hydrophobic Binding ◽  
Kinetics Of

The kinetics of the reactions of the active-centre thiol groups of papain (EC 3.4.22.2) and ficin (EC 3.4.22.3) with the two-protonic-state reactivity probes 2,2′-dipyridyl disulphide, n-propyl 2-pyridyl disulphide and 4-(N-aminoethyl 2′-pyridyl disulphide)- 7-nitrobenzo-2-oxa-1,3-diazole (compound I) were studied over a wide range of pH. Differences between the reactivities of ficin and papain towards the cationic forms of the alkyl 2-pyridyl disulphide probes suggest that ficin contains a cationic site without exact analogue in papain, and the striking difference in the shapes of the pH-rate profiles for the reactions of the two enzymes with compound (1) suggests differences in the mobilities or dispositions of the active-centre histidine imidazole groups with respect to relevant hydrophobic binding areas. The evidence from reactivity-probe studies that the papain catalytic mechanism involves substantial repositioning of the active-centre imidazole group during the catalytic act does not apply also to ficin. If ficin contains an aspartic acid residue analogous to aspartic acid-158 in papain, the pKa of its carboxy group is probably significantly lower than the pKa of the analogous group in papain.

Sign in / Sign up

Export Citation Format

Share Document