Dependence of in vitro Enzymic Hydrolysis of Alkyl(2-benzoyloxyethyl)dimethylammonium Bromides on the Alkyl Length

1998 ◽  
Vol 63 (2) ◽  
pp. 245-251 ◽  
Author(s):  
Eva Olaszová ◽  
Ingrid Paulíková ◽  
Otto Helia ◽  
Emil Švajdlenka ◽  
Ferdinand Devínský ◽  
...  
Keyword(s):  
Benzoic Acid ◽  
Alkyl Chain ◽  
Ammonium Nitrogen ◽  
Acid Formation ◽  
Ester Bond ◽  
Enzymic Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Alkyl Length

Microsomal esterases were used in the study of the in vitro enzymic hydrolysis of the ester bond in alkyl(2-benzoyloxyethyl)dimethylammonium bromides. These compounds are potential "soft" disinfectants, easily biodegradable to nontoxic biologically inactive hydrolytic products, namely substituted choline and benzoic acid. Formation of the latter product was used to monitor the kinetics of the reaction. It has been found that the rate of enzymic hydrolysis is substantially influenced by different length of the alkyl chain on the ammonium nitrogen. At the same time, interspecies (rat-mouse) and interorgan (liver-kidney) variability has been observed.

ChemInform Abstract: Dependence of in vitro Enzymic Hydrolysis of Alkyl(2-benzoyloxyethyl)dimethylammonium Bromides on the Alkyl Length.

ChemInform ◽  
2010 ◽  
Vol 29 (25) ◽  
pp. no-no
Author(s):  
E. OLASZOVA ◽  
I. PAULIKOVA ◽  
O. HELIA ◽  
E. SVAJDLENKA ◽  
F. DEVINSKY ◽  
...  
Keyword(s):  
Enzymic Hydrolysis ◽  
Hydrolysis Of ◽  
Alkyl Length

scholarly journals SIMILARITY OF THE KINETICS OF INVERTASE ACTION IN VIVO AND IN VITRO

1932 ◽  
Vol 15 (5) ◽  
pp. 491-495 ◽  
Author(s):  
J. M. Nelson ◽  
Elizabeth T. Palmer ◽  
B. G. Wilkes
Keyword(s):  
Yeast Cells ◽  
Enzymic Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Live Yeast

1. A method is given whereby the course of hydrolysis of sucrose by live yeast cells may be followed with precision equal to that found when invertase solutions prepared from autolyzed yeast are used to cause inversion. 2. The practical value of the equation of Nelson and Hitchcock as a means of following the course of enzymic hydrolysis of sucrose is hereby extended. 3. The inversion of sucrose by live yeast cells and by extracted invertase has been quantitatively compared. 4. The course of hydrolysis of sucrose by the invertase of Fleischmann's yeast has been found to be identical in vivo and in vitro.

Covalent attachment of amino acids to casein. 1. Chemical modification and rates of in vitro enzymic hydrolysis of derivatives

1979 ◽  
Vol 27 (5) ◽  
pp. 1098-1104 ◽  
Author(s):  
Antoine J. Puigserver ◽  
Lourminia C. Sen ◽  
Elvira Gonzales-Flores ◽  
Robert E. Feeney ◽  
John R. Whitaker
Keyword(s):  
Amino Acids ◽  
Chemical Modification ◽  
Covalent Attachment ◽  
Enzymic Hydrolysis ◽  
Hydrolysis Of

Effect of 2,4-D on the Hydrolysis of Diclofop-Methyl in Wild Oat (Avena fatua)

Weed Science ◽  
1980 ◽  
Vol 28 (6) ◽  
pp. 725-729 ◽  
Author(s):  
B. D. Hill ◽  
B. G. Todd ◽  
E. H. Stobbe
Keyword(s):  
Enzyme Preparation ◽  
Avena Fatua ◽  
Wild Oat ◽  
Enzymic Hydrolysis ◽  
Standard Assay ◽  
Rate Of Hydrolysis ◽  
Dichlorophenoxy Acetic Acid ◽  
Hydrolysis Of ◽  
Assay Conditions

The basis for 2,4-D [(2,4-dichlorophenoxy)acetic acid] antagonism of diclofop-methyl {methyl 2-[4-(2,4-dichlorophenoxy) phenoxy] propanoate} toxicity to wild oat (Avena fatuaL.) was investigated by studying changes in the metabolism of diclofop-methyl in vitro. An esterase from wild oat, which hydrolyzes diclofop-methyl to the acid diclofop, was extracted, partially purified, and the reaction characterized. The rate of hydrolysis of14C-diclofop-methyl was 0.14 ηmoles/2 h at standard assay conditions of 0.25 mg lyophilized enzyme preparation (19.6% protein) in 0.1 ml phosphate buffer (0.1 M, pH 7.0), substrate 5 μM. The addition of 2,4-D to this reaction did not inhibit14C-diclofop formation. Higher levels of 2,4-D stimulated enzymic hydrolysis.14C-diclofop-methyl was rapidly metabolized to14C-diclofop and polar14C-conjugates when vacuum-infiltrated into wild oat leaf segments. The addition of 2,4-D caused small increases in the rates of both14C-diclofop-methyl de-esterification and14C-diclofop conjugation. It is concluded that 2,4-D does not inhibit the in vitro de-esterification of diclofop-methyl.

Inhibitory action of somatostatin on isolated gastric glands and parietal cells

1983 ◽  
Vol 245 (2) ◽  
pp. G221-G229 ◽  
Author(s):  
C. S. Chew
Keyword(s):  
Parietal Cell ◽  
Inhibitory Action ◽  
Parietal Cells ◽  
Acid Formation ◽  
Gastric Glands ◽  
Isolated Gastric Glands ◽  
Cell Acid ◽  
Kinetics Of ◽  
Apparent Ic50

The action of somatostatin in vitro was characterized using glands and parietal cells isolated from rabbit gastric mucosa. In the presence of the reducing agent dithiothreitol, somatostatin was found to inhibit gastrin- and histamine-stimulated acid formation in glands as measured by [14C]aminopyrine (AP) accumulation and oxygen consumption, both measurements that appear to be reliable indexes of parietal cell acid formation. In glands the inhibition of the secretory response to gastrin was more potent (60-80%) than that to histamine (15-25%). The kinetics of somatostatin inhibition of responses to both agents were noncompetitive. The apparent IC50 for the partial somatostatin inhibition of histamine-stimulated AP accumulation was similar to that for gastrin (approx 3 X 10(-9) M) when maximum concentrations of histamine (10(-4) M) or gastrin (10(-7) M) were used. The inhibitory action of somatostatin appeared to be specific, inasmuch as this peptide had no significant effect on basal secretion or secretion stimulated by carbachol, dibutyryl cAMP, cholera toxin, or elevated extracellular K+. In purified parietal cell preparations, somatostatin inhibited histamine- but not gastrin-stimulated AP accumulation. Moreover, the inhibition of histamine-stimulated AP accumulation in parietal cells was more pronounced than in glands. These results suggest that somatostatin acts directly on parietal cells to inhibit histamine activation of H+ secretion. Somatostatin also acts indirectly to inhibit gastrin, perhaps by blocking the release of histamine from paracrine- or endocrinelike cells present in the glands.

Kinetics of a heterogeneous enzymic hydrolysis of a prochiral diester

1992 ◽  
Vol 57 (16) ◽  
pp. 4544-4546 ◽  
Author(s):  
George B. Smith ◽  
Mahadevan Bhupathy ◽  
George C. Dezeny ◽  
Alan W. Douglas ◽  
Russel J. Lander
Keyword(s):  
Enzymic Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of

Kinetics of enzymic hydrolysis of cassava flour starch - optimization and modelling

2007 ◽  
Vol 27 (4) ◽  
pp. 465-472 ◽  
Author(s):  
KRZYSZTOF N. WALISZWESKI ◽  
MIGUEL GARCIA ALVARADO ◽  
JAVIER DE LA CRUZ MEDINA
Keyword(s):  
Enzymic Hydrolysis ◽  
Cassava Flour ◽  
Kinetics Of ◽  
Hydrolysis Of

Kinetics of in Vitro Hydrolysis of Homocamptothecins As Measured by Fluorescence

2006 ◽  
Vol 922 (1) ◽  
pp. 314-316 ◽  
Author(s):  
D. CHAUVIER ◽  
I. CHOURPA ◽  
D. C.H. BIGG ◽  
M. MANFAIT
Keyword(s):  
In Vitro Hydrolysis ◽  
Kinetics Of ◽  
Hydrolysis Of

Enzymic Hydrolysis of Stilbestrol Diphosphate in vitro and in vivo.

1961 ◽  
Vol 106 (2) ◽  
pp. 327-330 ◽  
Author(s):  
W. Johnson ◽  
R. Jasmin ◽  
G. Corte
Keyword(s):  
Enzymic Hydrolysis ◽  
Hydrolysis Of
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