Cecal enzyme activity in gilts following experimentally induced Fusarium mycotoxicosis

2015 ◽  
Vol 18 (1) ◽  
pp. 191-197 ◽  
Author(s):  
K. Śliżewska ◽  
A. Nowak ◽  
M. Piotrowska ◽  
Z. Żakowska ◽  
M. Gajęcka ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
The Third ◽  
Activity Of Enzymes ◽  
Descending Colon ◽  
Experimentally Induced

AbstractThe objective of the presented study was to examine the influence ofFusariummycotoxins (zearalenone – ZEN and deoxynivalenol – DON), administered separately and in combination, on the activity of cecal enzymes (β-glucosidase and β-glucuronidase) in gilts which were fed fodder contaminated with these mycotoxins. The activity of β-glucosidase and β-glucuronidase varied in the range of 0.170-1.236 μmol · h−1· mg−1and 8.701-96.704 μmol · h−1· mg−1, respectively. In the first two weeks, the toxins had no significant effect on the activity of β-glucosidase and β-glucuronidase in the ascending and descending colon. After week 3 and later on, ZEN and DON administered as a mixture led to the highest increase in the activity of both enzymes. Administered separately, DON affected the activity of enzymes more than ZEN. From the third week of the experiment, an increase in the activity of CW β-glucosidase and β-glucuronidase was observed.

scholarly journals Effect of pesticide Glyphosate Aqua in liver enzymes activity of Barbus sharpeyi

2016 ◽  
Vol 13 (2) ◽  
pp. 240-246
Author(s):  
Baghdad Science Journal
Keyword(s):  
Liver Enzymes ◽  
Fish Nutrition ◽  
Control Group ◽  
Average Weight ◽  
Biochemical Tests ◽  
The Third ◽  
Nutrition Research ◽  
Barbus Sharpeyi ◽  
Activity Of Enzymes ◽  
And Control

The present study was designed in the aquaculture and fish nutrition research aquarium in the College of Veterinary Medicine/Baghdad University from a period 1/3 to 1/6/2013 to investigate the toxicity of the herbicide glyphosate aqua on Barbus sharpeyi fish. Fish fingerlings were used with average weight between 10 – 15 gm to measure the (LC50), and 200 fingerlings were used to know the acute and chronic toxic effect for the herbicide. The fingerlings were randomly distributed as 10 fish for each aquarium. Fish were divided into four treatments and control group (without addition of herbicide). The first processing with a concentration of 0.415 mg/L for a duration of exposure 90 days, the second processing group with a concentration 0.415 mg/L for 15 days, while the third group was treated with 0.207 mg/L of the herbicide for a duration of exposure, the forth group was exposed to 0.207 mg/L for 15 days only. The study aimed to determine the extent of the effect of the pesticide in the activity of liver enzymes, which included Alkaline phosphatase (ALP), Aspartate amino transfers (AST) and Alanine amino transfers (ALT). The results of biochemical tests for liver enzymes to fish experience has shown a rise in activity of enzymes which increased with duration of exposure. The first and the third treatments has a significant differences (P ?0.05) compared with control group. Results of the experiment to improvement in the health status of fish in second and forth treatments compared to control group.

Interaction between pyridine nucleotide coenzymes and heme proteins as a possible source of error in assay of activities of coenzyme-linked enzyme.

1989 ◽  
Vol 35 (10) ◽  
pp. 2129-2133 ◽  
Author(s):  
M D Jeyasingham ◽  
O E Pratt ◽  
H K Roopral
Keyword(s):  
Pyridine Nucleotide ◽  
Peak Height ◽  
Heme Group ◽  
Ultraviolet Absorbance ◽  
The Third ◽  
Spectral Shifts ◽  
Muscle Breakdown ◽  
Activity Of Enzymes ◽  
Source Of Error ◽  
Absorbance Spectra

Abstract The ultraviolet absorbance spectra of pyridine nucleotide coenzymes change in the presence of heme-containing proteins. The positions of each of the two main absorbance peaks of NADH are shifted progressively towards shorter wavelengths in the presence of increasing concentrations of hemoglobin, and the third peak, at 220 nm, disappears altogether. Similar changes are seen in the spectra of NAD+ and NADPH, and similar effects on these spectra are produced by myoglobin and cytochrome c, but not by comparable concentrations of albumin. The spectral shifts are generally accompanied by a decreased peak height. This finding may help explain problems reported by previous workers in the measurement of the activity of enzymes such as transketolase or lactate dehydrogenase in erythrocyte hemolysates. Errors may be considerable if allowance is not made for this effect, especially if the concentration of heme protein in the spectrophotometer cuvette much exceeds 1 g/L. The interaction appears to indicate some form of bonding, occurring generally between pyridine nucleotide coenzymes and the heme group in proteins. We relate the findings to measurement of activities of pyridine nucleotide-linked enzymes in erythrocyte lysates and in plasma containing myoglobin after muscle breakdown.

scholarly journals Influence of fullerenol C60(OH)24 on enzime status in serum of rats after single dose administration of doxorubicine

2008 ◽  
Vol 62 (3) ◽  
pp. 191-196 ◽  
Author(s):  
Biljana Govedarica ◽  
Vukosava Djordjevic-Milic ◽  
Natasa Radic ◽  
Branislava Srdjenovic ◽  
Aleksandar Djordjevic
Keyword(s):  
Enzyme Activity ◽  
Single Dose ◽  
Free Radicals ◽  
Side Effects ◽  
Topoisomerase Ii ◽  
Control Group ◽  
Limiting Factor ◽  
Dose Administration ◽  
Activity Of Enzymes

The antracycline antibiotics have one of the widest areas of use in oncology. The most investigated mechanisms of their antineoplastic activity include: interactions of these antibiotics with DNA, inhibition of topoisomerase II and production of free radicals. However, the side effects of doxorubicin, especially cardiotoxicity, are the limiting factor of its use in cancer therapy. The aim of this research was to investigate the influence of fullerenol ?60(?H)24 as a cytoprotector in single doze administration of doxorubicin on the activity of enzymes in serum (CK, AST, ALT, LDH and a-HBDH) in rats in in vivo system. Activity of enzymes (CK, LDH, HBDH, AST, and ALT) in serume was measured with standard commercial methods. The results of analysis of the samples treated with the combination of fullerenol and doxorubicin show no difference in enzyme activity in comparison with the control group. The results indicate the possibility of using fullerenol as a protector in the therapy with doxorubicin in malign neoplasm.

THE ACTIVITY OF ENZYMES IN THE RABBIT UTERUS AND EFFECT OF PROGESTERONE AND OESTRADIOL

1969 ◽  
Vol 43 (2) ◽  
pp. 167-174 ◽  
Author(s):  
R. N. MURDOCH ◽  
I. G. WHITE
Keyword(s):  
Alkaline Phosphatase ◽  
Enzyme Activity ◽  
Succinic Dehydrogenase ◽  
Lactic Dehydrogenase ◽  
Glutamate Oxaloacetate Transaminase ◽  
Oestrogen Treatment ◽  
Uterine Endometrium ◽  
Uterine Fluid ◽  
Activity Of Enzymes ◽  
Glucose 6 Phosphate Dehydrogenase

SUMMARY The activity of several enzymes has been measured in the uterine endometrium of the rabbit during oestrus and pseudopregnancy and after injecting oestradiol benzoate or progesterone 28 days after ovariectomy. The enzyme activity of the uterine fluid has been determined during oestrus and the effect of uterine ligation studied. Progesterone and the induction of pseudopregnancy stimulated succinic dehydrogenase (SDH) and glucose-6-phosphate dehydrogenase (GDH) activity and depressed amylase and lactic dehydrogenase (LDH) activity. In ovariectomized does, glutamate-oxaloacetate transaminase (GOT) activity increased after the injection of progesterone. Progesterone also stimulated endometrial phosphatase after ovariectomy but, when given after a period of oestrogen treatment, it limited the even greater response of acid and alkaline phosphatase to oestrogen; the activity then attaining the same level as when progesterone alone was given. SDH, GDH and glycerylphosphorylcholine (GPC) diesterase could not be detected in uterine fluid but amylase and alkaline phosphatase were in greater concentration than in the endometrium. GPC diesterase was, however, found to be present in uterine tissue. Ligation of the uterus did not significantly alter the enzyme activity of the endometrium.

scholarly journals SEGMENTAL ANEUPLOIDY AND ENZYME ACTIVITY AS A METHOD FOR CYTOGENETIC LOCALIZATION IN DROSOPHILA MELANOGASTER

Genetics ◽  
1974 ◽  
Vol 76 (2) ◽  
pp. 301-309
Author(s):  
Barbara R Stewart ◽  
John R Merriam
Keyword(s):  
Enzyme Activity ◽  
X Chromosome ◽  
Gene Dosage ◽  
Chromosome Region ◽  
Structural Genes ◽  
The Third ◽  
Segmental Aneuploidy ◽  
Cytological Localization ◽  
The Relationship ◽  
Chromosome Bands

ABSTRACT A method of mapping genes which specify enzymes without the necessity of obtaining genetic variants has been explored. Three enzymes whose structural genes have known genetic positions were chosen to see if the relationship between gene dosage and enzyme activity could be used as a tool in cytological localization. Zw, the gene specifying G6PD, is located in the X chromosome region, 18D-18F. The structural gene for 6PGD, Pgd, maps in the X chromosome bands 2C1-2E1. Idh-NADP, the gene which specifies IDH-NADP, is found on the third chromosome, in bands 66B-67C.

scholarly journals The Role of Acetylcholine Esterase in Resistance Mechanism of Plutella xylostella to Emamektin Benzoate

2018 ◽  
Vol 10 (1) ◽  
pp. 66-71
Author(s):  
Udi Tarwotjo ◽  
Rully Rahadian
Keyword(s):  
Enzyme Activity ◽  
Esterase Activity ◽  
Resistance Mechanism ◽  
Acetylcholinesterase Activity ◽  
Acetylcholine Esterase ◽  
Emamectin Benzoate ◽  
Susceptible Population ◽  
The Third ◽  
Naphthyl Acetate

One of the resistance mechanism of P. xylostellato emamektin benzoate is target insensitivity which is acetylcholine esterase that responsible for resistance occurrence. The objective of this study was to determine the role of acetylcholinesterase in the resistance mechanism of P. xylostella population to emamektin benzoate. For enzyme activity analysis, larvae homogenate of the third instar of P. xylostella was prepared. The number of insects required for each scour is 1 for each field population. The protein content in P. xylostella homogenate was measured by the Folin-Ciocalteu test. Non-specific esterase activity with an absorption rate was read using ELISA reader tool with λ = 450 nm. The inhibition level of acetylcholinesterase activity by emamectin benzoate in the tested population was 36.84%. The highest inhibition occurs in Puasan (Ngablak) population.  The result shows that a α-naphthyl acetate substrate was used so that it was recorded as non-specific esterase activity and did not exhibit esterase activity which specifically describes emamectin benzoate. Non-specific esterase enzyme activity of either α or β-naphthyl acetate substances to benzoic emamectin in the tested population most of the population was still susceptible. On α-naphthyl acetate substrate, the highest absorbance value found in susceptible population to benzoate emamectin (0.773), while the lowest found in Babrik (Ngablak) population  (0.083).

scholarly journals Crystal structures of Aspergillus oryzae Rib2 deaminase: the functional mechanism involved in riboflavin biosynthesis

IUCrJ ◽  
2021 ◽  
Vol 8 (4) ◽  
Author(s):  
Sheng-Chia Chen ◽  
Li-Ci Ye ◽  
Te-Ming Yen ◽  
Ruei-Xin Zhu ◽  
Cheng-Yu Li ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
High Resolution ◽  
Protein Stability ◽  
Crystal Structures ◽  
Aspergillus Oryzae ◽  
Terminal Segment ◽  
Riboflavin Biosynthesis ◽  
The Third ◽  
Complex Forms ◽  
Deaminase Domain

Riboflavin serves as the direct precursor of the FAD/FMN coenzymes and is biosynthesized in most prokaryotes, fungi and plants. Fungal Rib2 possesses a deaminase domain for deamination of pyrimidine in the third step of riboflavin biosynthesis. Here, four high-resolution crystal structures of a Rib2 deaminase from Aspergillus oryzae (AoRib2) are reported which display three distinct occluded, open and complex forms that are involved in substrate binding and catalysis. In addition to the deaminase domain, AoRib2 contains a unique C-terminal segment which is rich in charged residues. Deletion of this unique segment has no effect on either enzyme activity or protein stability. Nevertheless, the C-terminal αF helix preceding the segment plays a role in maintaining protein stability and activity. Unexpectedly, AoRib2 is the first mononucleotide deaminase found to exist as a monomer, perhaps due to the assistance of its unique longer loops (Lβ1–β2, LαB–β3 and LαC–β4). These results form the basis for a molecular understanding of riboflavin biosynthesis in fungi and might assist in the development of antibiotics.

scholarly journals Ozonized solutions favor the repair of experimentally induced skin wounds in rats

2020 ◽  
Vol 40 (11) ◽  
pp. 914-921
Author(s):  
Rafael C. Sanguanini ◽  
Mariana F. Bento ◽  
Evelyn de Oliveira ◽  
Emmanuel Arnhold ◽  
Mariana B.R. Faleiro ◽  
...  
Keyword(s):  
Sodium Chloride ◽  
Tissue Repair ◽  
Wound Repair ◽  
Type I Collagen ◽  
Type I ◽  
Skin Wounds ◽  
The Third ◽  
Picrosirius Red ◽  
Morphometric Evaluation ◽  
Experimentally Induced

ABSTRACT: This study aimed to evaluate and compare the effects of ozonized solutions on tissue wound repair in rats. Treatments consisted of ozonized water (GA), 0.9% sodium chloride (GCL), ozonized oil (GO), and 0.2% allantoin cream (GAL). The morphometric evaluation showed that wounds of the GA group presented a higher degree of retraction (p<0.05) at three and eight days of treatment (37.96 and 84.81%, respectively). Picrosirius red staining showed that groups GA and GO presented higher deposition (p<0.05) of type I collagen at 15 and 22 days of treatment, respectively. The neovascularization was higher in wounds of group GO on days 3, 8, and 15 (p<0.05), with higher VEGF immunostaining. (p<0.05). Thus, ozonized water enhances wound retraction and assists in the maturation and remodeling phase, while ozonized oil promotes higher neovascularization during tissue repair and higher deposition of type I collagen from the third week of treatment.

Immunochemical properties of immunoglobulin G conjugated with lactate dehydrogenase.

1985 ◽  
Vol 31 (7) ◽  
pp. 1178-1181 ◽  
Author(s):  
K Sudo ◽  
M Maekawa ◽  
T Kanno
Keyword(s):  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Immunoglobulin G ◽  
Equilibrium Constants ◽  
Antigen Recognition ◽  
Binding Affinities ◽  
Rabbit Antibody ◽  
Human Igg ◽  
The Third ◽  
Enzyme Molecules

Abstract Quantitative binding affinities of immunoglobulin G (IgG) for the five isoenzymes of lactate dehydrogenase (LD; EC 1.1.1.27) were determined for IgG isolated from three patients' sera that contained LD-IgG complexes. These three IgGs formed soluble complexes with four (LD 1, 2, 3, 5) of the five LD isoenzymes in two of the patients and in the third they bound with three (LD 2, 3, 4) of the five LD isoenzymes without inhibiting the enzyme activity or precipitating with the enzyme molecules. When rabbit antibody to human IgG was added to these sera, the complexes between the LD isoenzymes and the patients' isolated IgG were completely precipitated. The equilibrium constants for the respective isolated IgG complexes with LD-3 were 0.102, 2.58, and 7.49 X 10(8) L/mol. In these three cases, LD-3 evoked the strongest response from the prepared IgG, demonstrating that the site of antigen recognition of LD-linked IgG was not associated with the structure of individual H and M subunits.

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