scholarly journals Nitrification inhibitor reduces the inhibitory effect of N‐(n‐butyl) thiophosphoric triamide (NBPT) on the hydrolysis of urea

2020 ◽  
Vol 84 (5) ◽  
pp. 1782-1794
Author(s):  
Ahmed A. Lasisi ◽  
Olalekan O. Akinremi ◽  
Darshani Kumaragamage
Keyword(s):  
Nitrification Inhibitor ◽  
Inhibitory Effect ◽  
Hydrolysis Of ◽  
Hydrolysis Of Urea

scholarly journals Evidence for the regulation of guinea-pig heart microsomal phosphatidylcholine-hydrolysing phospholipase A1 by guanosine 5′-[γ-thio]triphosphate

1992 ◽  
Vol 288 (3) ◽  
pp. 965-968 ◽  
Author(s):  
K Badiani ◽  
X Lu ◽  
G Arthur
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Guinea Pig ◽  
Molecular Species ◽  
Inhibitory Effect ◽  
Phospholipase A1 ◽  
Guinea Pig Heart ◽  
Substrate Specificities ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of

We have recently characterized lysophospholipase A2 activities in guinea-pig heart microsomes and postulated that these enzymes act sequentially with phospholipases A1 to release fatty acids selectively from phosphatidylcholine (PC) and phosphatidylethanolamine, thus providing an alternative route to the phospholipase A2 mode of release. In a further investigation of the postulated pathway, we have characterized the PC-hydrolysing phospholipase A1 in guinea-pig heart microsomes. Our results show that the enzyme may have a preference for substrates with C16:0 over C18:0 at the sn-1 position. In addition, although the enzyme cleaves the sn-1 fatty acid, the rate of hydrolysis of PC substrates with C16:0 at the sn-1 position was influenced by the nature of the fatty acid at the sn-2 position. The order of decreasing preference was C18:2 > C20:4 = C18:1 > C16:0. The hydrolyses of the molecular species were differentially affected by heating at 60 degrees C. An investigation into the effect of nucleotides on the activity of the enzyme showed that guanosine 5′-[gamma-thio]triphosphate (GTP[S]) inhibited the hydrolysis of PC by phospholipase A1 activity, whereas GTP, guanosine 5′-[beta-thio]diphosphate (GDP[S]), GDP, ATP and adenosine 5′-[gamma-thio]triphosphate (ATP[S]) did not affect the activity. The inhibitory effect of GTP[S] on phospholipase A1 activity was blocked by preincubation with GDP[S]. A differential effect of GTP[S] on the hydrolysis of different molecular species was also observed. Taken together, the results of this study suggest the presence of more than one phospholipase A1 in the microsomes with different substrate specificities, which act sequentially with lysophospholipase A2 to release linoleic or arachidonic acid selectively from PC under resting conditions. Upon stimulation and activation of the G-protein, the release of fatty acids would be inhibited.

Hydrolysis of phosphatidylcholine couples Ras to activation of Raf protein kinase during mitogenic signal transduction

1993 ◽  
Vol 13 (12) ◽  
pp. 7645-7651
Author(s):  
H Cai ◽  
P Erhardt ◽  
J Troppmair ◽  
M T Diaz-Meco ◽  
G Sithanandam ◽  
...  
Keyword(s):  
Growth Factors ◽  
Protein Kinase ◽  
Inhibitory Effect ◽  
Dominant Negative ◽  
Expression Plasmid ◽  
Quiescent Cells ◽  
Mitogenic Signal Transduction ◽  
The Relationship ◽  
Hydrolysis Of ◽  
Mitogenic Signal

We have investigated the relationship between hydrolysis of phosphatidylcholine (PC) and activation of the Raf-1 protein kinase in Ras-mediated transduction of mitogenic signals. As previously reported, cotransfection of a PC-specific phospholipase C (PC-PLC) expression plasmid bypassed the block to cell proliferation resulting from expression of the dominant inhibitory mutant Ras N-17. In contrast, PC-PLC failed to bypass the inhibitory effect of dominant negative Raf mutants, suggesting that PC-PLC functions downstream of Ras but upstream of Raf. Consistent with this hypothesis, treatment of quiescent cells with exogenous PC-PLC induced Raf activation, even when normal Ras function was blocked by Ras N-17 expression. Further, activation of Raf in response to mitogenic growth factors was blocked by inhibition of endogenous PC-PLC. Taken together, these results indicate that hydrolysis of PC mediates Raf activation in response to mitogenic growth factors.

Hydrocortisone inhibits mucin secretion from guinea pig gallbladder

1984 ◽  
Vol 247 (4) ◽  
pp. G427-G431 ◽  
Author(s):  
J. R. Moore ◽  
B. S. Turner ◽  
J. T. LaMont
Keyword(s):  
Guinea Pig ◽  
Phospholipase A2 ◽  
Sodium Succinate ◽  
Inhibitory Effect ◽  
Membrane Phospholipids ◽  
Mucin Secretion ◽  
Basal Secretion ◽  
Prostaglandin Release ◽  
Hydrolysis Of

We studied the effects of hydrocortisone, an inhibitor of phospholipase A2, on the secretion of mucin and release of prostaglandins from guinea pig gallbladder explants. We measured mucin using [3H]glucosamine as a precursor and prostaglandins by radioimmunoassay of 6-keto-prostaglandin F1 alpha. Mucin secretion and prostaglandin release were studied under basal conditions and after arachidonate stimulation. Hydrocortisone sodium succinate reversibly inhibited basal secretion of mucin by 24% at 10(-5) M (P less than 0.05 compared with control) and 34% at 10(-4) M (P less than 0.01). Hydrocortisone, 10(-4) M, also reversibly inhibited arachidonate-stimulated secretion of mucin (P less than 0.01 compared with controls incubated with arachidonate alone). Release of prostaglandin F1 alpha was significantly inhibited by hydrocortisone under basal (P less than 0.01) and arachidonate-stimulated (P less than 0.01) conditions. The inhibitory effect of hydrocortisone was mediated by inhibition of hydrolysis of arachidonate from membrane phospholipids, suggesting that exogenous arachidonate is incorporated into membrane phospholipids prior to conversion to prostaglandins.

Inhibitory effect of soil humic compounds on the proteolytic enzyme pronase

Soil Research ◽  
1969 ◽  
Vol 7 (3) ◽  
pp. 241
Author(s):  
JN Ladd ◽  
JHA Butler
Keyword(s):  
Humic Acids ◽  
Maximum Velocity ◽  
Kinetic Studies ◽  
Inhibitory Effect ◽  
Enzymic Activity ◽  
Humic Compounds ◽  
Km Value ◽  
Group Basis ◽  
Inhibitory Power ◽  
Hydrolysis Of

Neutralized solutions of soil humic acids inhibit the proteolytic activity of the enzyme pronase when tested against a variety of substrates. Protein hydrolysis was less sensitive than hydrolysis of dipeptide derivatives; 50% inhibition of benzyloxycarbonylglycylleucine hydrolysis was achieved with concentrations of humic acids as low as 1-2 �g/ml or less than 10-5M, on a carboxyl group basis. Humic acids, extracted from soils with different crop histories, showed only slight differences in their effectiveness as inhibitors of pronase activity. Their inhibitory power was comparable with that of other high molecular weight polyanions, e.g. polyacrylic acid and polycondensates derived from p-benzoquinone and catechol. Alginic acid was a relatively poor inhibitor. Preincubation of humic acids for various periods with either pronase or substrate (albumin or benzyloxycarbonylglycylleucine) had little or no effect on the subsequent inhibition of enzymic activity. However, inhibition is decreased by increasing substrate concentrations, following preincubation of humic acids and pronase. Both observations are consistent with a reversible inhibitory mechanism. Kinetic studies demonstrate that humic acids inhibit pronase activity towards albumin and N-benzyloxycarbonyl dipeptides by effectively reducing the affinity of pronase for the substrate, i.e. by increasing the Km value for the reaction. With benzoylarginine amide and benzoylarginine ethyl ester as substrates, the reaction velocity is lowered due to a reduction of the maximum velocity of the system. Both effects may possibly be explained by a conformational change in the enzyme structure due to combination with the humic acid molecules.

scholarly journals Discussion on the Scheme of Preparing Ammonia Gas by Hydrolysis of Urea

2019 ◽  
Vol 612 ◽  
pp. 042034
Author(s):  
Jingcheng Su ◽  
Fangming Xue ◽  
Feng Chen ◽  
Yiqing Sun ◽  
Xiuru Liu
Keyword(s):  
Ammonia Gas ◽  
Hydrolysis Of ◽  
Hydrolysis Of Urea

The differentiation of Trichophyton rubrum and T. mentagrophytes by use of Christensen's urea broth

1971 ◽  
Vol 17 (7) ◽  
pp. 911-913 ◽  
Author(s):  
Julius Kane ◽  
J. B. Fischer
Keyword(s):  
Urease Activity ◽  
Trichophyton Rubrum ◽  
Agar Medium ◽  
Phenol Red ◽  
Depressing Effect ◽  
Fluid Medium ◽  
Maximum Change ◽  
Pure Cultures ◽  
Hydrolysis Of ◽  
Hydrolysis Of Urea

A comparison of the urease activity of 56 strains of T. rubrum and 64 strains of T. mentagrophytes on Christensen's urea medium with and without agar incubated 7 days at 28 °C showed that characteristic and consistent results are produced on this medium without agar. In the fluid medium T. mentagrophytes caused a rise in pH, resulting in a maximum change of the phenol red, and T. rubrum produced no change. The depressing effect of agar on the hydrolysis of urea was demonstrated. On the agar medium 9 (18.8%) of 48 strains of T. mentagrophytes and 3 (6.2%) of 48 strains of T. rubrum produced doubtful results. It is important that pure cultures be used for the test.

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