In-Vitro Effects of Ricinus Communis Seed Kernel Extract On Some Antioxidant And Hydrolytic Enzymes In Nymph And Adult Zonocerus Variegatus (Grasshopper)

2019 ◽  
Vol 3 (1) ◽  
pp. 129-137
Author(s):  
Gbadebo E . Adeleke ◽  
Olaniyi T. Adedosu ◽  
Rachael O. Adeyi ◽  
John O. Fatoki
Keyword(s):  
Ricinus Communis ◽  
Hydrolytic Enzymes ◽  
Crude Enzyme ◽  
Economic Losses ◽  
Seed Kernel ◽  
Zonocerus Variegatus ◽  
Sod Activity ◽  
Enzyme Preparations ◽  
In Vitro Effects

Background: Many plants have been identified for their insecticidal properties as alternatives to synthetic ones, which are toxic to untargeted organisms and environment. Ricinus communis (Castor) has been re-ported to exhibit insecticidal properties against insect pests. Zonocerus variegatus (Grasshopper) is a notable pest of several crops, and has been linked with great economic losses to farmers. The present study investigates the in-vitro toxicity of R. communis seed kernel extract (RCSKE) on the activities of selected antioxidant and hydrolytic enzymes in nymph and adult Zonocerus variegatus (Grasshopper), using cypermethrin (CYPER-M) and chlorpyrifos (CPF) as standard conventional pesticides. Methods: Seed kernel of Ricinus communis (Castor) was subjected to acidified aqueous extraction to obtain the extract (RCSKE). Crude enzyme preparations were obtained from nymph and adult Z. variegatus grass-hoppers. The in-vitro effects of different concentrations (15, 30, 45, 60, 75, 90 and 105μg/ml) each of RCSKE, CYPER-M and CPF on the activities of superoxide dismutase (SOD), catalase (CAT), acetylcholinesterase (AChE) and carboxylesterase (CES) in crude enzyme preparations were estimated spectrophotometrically. The level of statistical significance was 0.05. Results: The RCSKE significantly reduced the in-vitro SOD activity (p < 0.05) in nymph Z. variegatus at all the concentrations, whereas both CYPER-M and CPF significantly reduced the activity only at certain concentrations. The CAT activity in the nymph was significantly decreased by RCSKE and CPF at all the concentrations, but CYPER-M decreased it only at certain concentrations. In adult Z. variegatus, SOD activity was not significantly affected (p > 0.05), while CAT activity was significantly increased (p < 0.05) by the three agents at all the concentrations. The AChE and CES activities in the nymph were significantly reduced by RCSKE, CYPER-M and CPF at all the concentrations. The RCSKE and CPF significantly increased the CES activity, while CYPER-M caused a significant decrease in the activity in adult Z. variegatus. Conclusion: The seed kernel extract of Ricinus communis is an effective pesticidal agent and hence, it could be a source of biopesticide alternative with greater potential than cypermethrin and chlorpyrifos. In addition, the antioxidant, acetylcholinesterase and carboxylesterase enzymes in the nymphs of Z. variegatus grasshoppers are more susceptible to the effect of the extract than in the adult grasshoppers.

scholarly journals Cell‐free in vitro reduction of carboxylates to aldehydes: With crude enzyme preparations to a key pharmaceutical building block

2020 ◽  
pp. 2000315
Author(s):  
Anna Schwarz ◽  
Sebastian Hecko ◽  
Florian Rudroff ◽  
Jeffrey T. Kohrt ◽  
Roger M. Howard ◽  
...  
Keyword(s):  
Building Block ◽  
Crude Enzyme ◽  
Enzyme Preparations

IN VITRO EFFECTS OF SUBSTITUTED IODOPHENOLS ON CATECHOL-O-METHYLTRANSFERASE

1963 ◽  
Vol 41 (8) ◽  
pp. 1779-1784 ◽  
Author(s):  
A. D'Iorio ◽  
C. Mavrides
Keyword(s):  
Kinetic Study ◽  
Enzyme Preparation ◽  
Crude Enzyme ◽  
Present Series ◽  
Hydroxybenzoic Acid ◽  
Reversible Inhibition ◽  
Crude Enzyme Preparation ◽  
Series Of Experiments ◽  
In Vitro Effects

The kinetic study of a new inhibitor of catechol-O-methyltransferase, 3,5-diiodo-4-hydroxybenzoic acid (DIHBA), previously reported by the authors (1), shows it to act in a competitive fashion. Instead of the crude enzyme preparation of the early experiments, a partially purified enzyme has been used throughout the present series of experiments and new substances have been tested with respect to their inhibiting effects. Thus, O-methyl-DIHBA is found to be inactive, while 3,5-diiodosalicylic acid (DISA) inhibits competitively and 3,5-diiodo-4-hydroxypyridine (DIHP) noncompetitively as indicated by the Lineweaver and Burk plots.3,5-Diiodo-4-hydroxyphenylpyruvic acid (DIHPA) produces a progressive and partly reversible inhibition, while 3,5-diiodotyrosine (DIT) has no effect on the activity of the enzyme. m-Fluorotyrosine, o-fluorophenol, and o-iodophenol are similarly inactive.

scholarly journals Hydrolytic enzymes and biodeterioration of groundnut seeds

2020 ◽  
Vol 26 (2) ◽  
Author(s):  
R.S. Deshmukh
Keyword(s):  
Aspergillus Flavus ◽  
Aspergillus Terreus ◽  
Hydrolytic Enzymes ◽  
Sclerotium Rolfsii ◽  
Macrophomina Phaseolina ◽  
Crude Enzyme ◽  
Protease Production ◽  
Enzyme Preparations ◽  
Fungal Isolates ◽  
The Media

Some common seed borne fungal isolates of Groundnut variety TAG-24 and SB-XI were screened for their ability to produce the hydrolytic enzymes. For this the test seed borne fungal isolates of Groundnut were grown on substrate and nonsubstrate glucose nitrate media for seven days at room temperature. After seven days of incubation the culture filtrates were collected separately and considered them as the crude enzyme preparation. The crude enzyme preparations were assayed by different methods under different conditions. Both varieties of Groundnut Aspergillus terreus and Sclerotium rolfsii were found to be highly amlolytic. All the test isolates of the Groundnut variety TAG-24 and SB-XI produced protease in both the media. Maximum protease production was found by Aspergillus flavus followed by Fusarium oxysporum. All the test isolates produced cellulase in both the media. Maximum cellulase production was found in Sclerotium rolfsii followed by Aspergillus niger and Aspergillus terreus. Among the seven test isolates Aspergillus flavus, Aspergillus terreus, Macrophomina phaseolina could not produce pectinase in the absence of substrate but the production was observed in the presence of substrate

IN VITRO EFFECTS OF SUBSTITUTED IODOPHENOLS ON CATECHOL-O-METHYLTRANSFERASE

1963 ◽  
Vol 41 (1) ◽  
pp. 1779-1784
Author(s):  
A. D'Iorio ◽  
C. Mavrides
Keyword(s):  
Kinetic Study ◽  
Enzyme Preparation ◽  
Crude Enzyme ◽  
Present Series ◽  
Hydroxybenzoic Acid ◽  
Reversible Inhibition ◽  
Crude Enzyme Preparation ◽  
Series Of Experiments ◽  
In Vitro Effects

The kinetic study of a new inhibitor of catechol-O-methyltransferase, 3,5-diiodo-4-hydroxybenzoic acid (DIHBA), previously reported by the authors (1), shows it to act in a competitive fashion. Instead of the crude enzyme preparation of the early experiments, a partially purified enzyme has been used throughout the present series of experiments and new substances have been tested with respect to their inhibiting effects. Thus, O-methyl-DIHBA is found to be inactive, while 3,5-diiodosalicylic acid (DISA) inhibits competitively and 3,5-diiodo-4-hydroxypyridine (DIHP) noncompetitively as indicated by the Lineweaver and Burk plots.3,5-Diiodo-4-hydroxyphenylpyruvic acid (DIHPA) produces a progressive and partly reversible inhibition, while 3,5-diiodotyrosine (DIT) has no effect on the activity of the enzyme. m-Fluorotyrosine, o-fluorophenol, and o-iodophenol are similarly inactive.

Anti-obesity role of Aster glehni extract: in vivo and in vitro effects

Planta Medica ◽  
2012 ◽  
Vol 78 (11) ◽  
Author(s):  
HM Lee ◽  
TG Ahn ◽  
CW Kim ◽  
HJ An
Keyword(s):  
In Vitro Effects

In Vitro Effects of Urokinase — Prevention by Different Inhibitors

1990 ◽  
Vol 64 (03) ◽  
pp. 402-406 ◽  
Author(s):  
M D Oethinger ◽  
E Seifried
Keyword(s):  
In Vitro Study ◽  
Thrombin Time ◽  
Plasma Samples ◽  
Temperature Dependent ◽  
Chloromethyl Ketone ◽  
Control Value ◽  
Dose Time ◽  
In Vitro Effects ◽  
Full Protection

SummaryThe present in vitro study investigated dose-, time- and temperature-dependent effects of two-chain urokinase plasminogen activato(u-PA, urokinase) on normal citrated plasma. When 10 μg/ml u-PA wereadded to pooled normal plasma and incubated for 30 min at an ambient temperature (25° C), α2-antiplas-min decreased to 8% of the control value. Incubation on ice yielded a decrease to 45% of control,whereas α2-antiplasmin was fully consumed at 37° C. Fibrinogen and plasminogen fell to 46% and 39%, respectively, after a 30 min incubation at 25° C. Thrombin time prolonged to 190% of control.Various inhibitors were studied with respect to their suitability and efficacy to prevent these in vitro effects. Aprotinin exhibited a good protective effect on fibrinogen at concentrations exceeding 500 KlU/ml plasma. Its use, however, was limited due to interferences with some haemostatic assays. We could demonstrate that L-Glutamyl-L-Glycyl-L-Arginyl chloromethyl ketone (GGACK) and a specific polyclonal anti-u-PA-antibody (anti-u-PA-IgG) effectively inhibited urokinase-induced plasmin generation without interfering with haemostatic assays. The anti-u-PA-antibody afforded full protection ofα2-antiplasmin at therapeutic levels of u-PA.It is concluded that u-PA in plasma samples from patients during thrombolytic therapy may induce in vitro effects which should be prevented by the use of a suitable inhibitor such as GGACK or specific anti-u-PA-antibody.

In Vitro Effects of Ethanol on Rabbit Platelet Aggregation, Secretion of Granule Contents, and Cyclic AMP Levels in the Presence of Prostacyclin

1989 ◽  
Vol 61 (02) ◽  
pp. 254-258 ◽  
Author(s):  
Margaret L Rand ◽  
Peter L Gross ◽  
Donna M Jakowec ◽  
Marian A Packham ◽  
J Fraser Mustard
Keyword(s):  
Cyclic Amp ◽  
Inhibitory Effect ◽  
Rabbit Platelet ◽  
Inhibitory Effects ◽  
Low Concentrations ◽  
Rabbit Platelets ◽  
High Concentrations ◽  
In Vitro Effects ◽  
Aggregation Of Platelets

SummaryEthanol, at physiologically tolerable concentrations, inhibits platelet responses to low concentrations of collagen or thrombin, but does not inhibit responses of washed rabbit platelets stimulated with high concentrations of ADP, collagen, or thrombin. However, when platelet responses to high concentrations of collagen or thrombin had been partially inhibited by prostacyclin (PGI2), ethanol had additional inhibitory effects on aggregation and secretion. These effects were also observed with aspirin- treated platelets stimulated with thrombin. Ethanol had no further inhibitory effect on aggregation of platelets stimulated with ADP, or the combination of ADP and epinephrine. Thus, the inhibitory effects of ethanol on platelet responses in the presence of PGI2 were very similar to its inhibitory effects in the absence of PGI2, when platelets were stimulated with lower concentrations of collagen or thrombin. Ethanol did not appear to exert its inhibitory effects by increasing cyclic AMP above basal levels and the additional inhibitory effects of ethanol in the presence of PGI2 did not appear to be brought about by further increases in platelet cyclic AMP levels.

Comparison of Specific Antibody, D-Phe-Pro-Arg-CH2Cl and Aprotinin for Prevention of In Vitro Effects of Recombinant Tissue-Type Plasminogen Activator on Haemostasis Parameters

1987 ◽  
Vol 58 (03) ◽  
pp. 921-926 ◽  
Author(s):  
E Seifried ◽  
P Tanswell
Keyword(s):  
Specific Antibody ◽  
Plasma Concentrations ◽  
Fibrinolytic Therapy ◽  
Tissue Type ◽  
Control Value ◽  
Type Plasminogen Activator ◽  
In Vitro Effects ◽  
Fibrinolytic Parameters

SummaryIn vitro, concentration-dependent effects of rt-PA on a range of coagulation and fibrinolytic assays in thawed plasma samples were investigated. In absence of a fibrinolytic inhibitor, 2 μg rt-PA/ml blood (3.4 μg/ml plasma) caused prolongation of clotting time assays and decreases of plasminogen (to 44% of the control value), fibrinogen (to 27%), α2-antiplasmin (to 5%), FV (to 67%), FVIII (to 41%) and FXIII (to 16%).Of three inhibitors tested, a specific polyclonal anti-rt-PA antibody prevented interferences in all fibrinolytic and most clotting assays. D-Phe-Pro-Arg-CH2Cl (PPACK) enabled correct assays of fibrinogen and fibrinolytic parameters but interfered with coagulometric assays dependent on endogenous thrombin generation. Aprotinin was suitable only for a restricted range of both assay types.Most in vitro effects were observed only with rt-PA plasma concentrations in excess of therapeutic values. Nevertheless it is concluded that for clinical application, collection of blood samples on either specific antibody or PPACK is essential for a correct assessment of in vivo effects of rt-PA on the haemostatic system in patients undergoing fibrinolytic therapy.

Observations on the in vitro Effects of Chylomicra, Low-Density Lipoproteins and Phospholipids on Human Plasma Euglobulin Lysis

1963 ◽  
Vol 09 (01) ◽  
pp. 164-174 ◽  
Author(s):  
Albert R Pappenhagen ◽  
J. L Koppel ◽  
John H Olwin
Keyword(s):  
Human Plasma ◽  
Phosphatidyl Ethanolamine ◽  
Phosphatidyl Inositol ◽  
Plasma Lipoproteins ◽  
Low Density ◽  
Inhibitory Effects ◽  
Soybean Phospholipids ◽  
In Vitro Effects ◽  
Complete Precipitation

SummaryData have been presented on the in vitro effects of human chylomicra, low-density human plasma lipoproteins, and partially purified preparations of various phospholipids on human plasma euglobulin lysis. Euglobulin lysis was found to be accelerated by preparations of mixed soybean phospholipids (aso-lectin), cephalin, phosphatidyl inositol, phophatidyl serine and phosphatidyl ethanolamine. In contrast, it was found to be inhibited by preparations of human chylomicra, low-density human plasma liproproteins and lecithin. Inhibition of euglobulin lysis produced by any of these three agents could be diminished or completely overcome by the simultaneous presence of suitable levels of any one of the accelerating agents. In all cases studied, both inhibitory and accelerating effects were observed to be concentration-dependent. Evidence has been obtained to suggest that in the case of the accelerating agents the observed increased rate of euglobulin lysis is not a direct effect on lysis itself, but rather is due to more complete precipitation of plasminogen in the presence of these substances. On the other hand, it appears that the inhibitory effects observed are not related to the extent of plasminogen precipitation, but are actually true inhibitions of euglobulin lysis. The possible clinical significance of some of these observations has been briefly discussed.

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