scholarly journals Biochemical Effects to Toxicity of CCl4 on Rosy Barbs (Puntius conchonius)

Our Nature ◽  
1970 ◽  
Vol 3 (1) ◽  
pp. 20-25 ◽  
Author(s):  
H. Bhattacharya ◽  
L. Lun ◽  
G.D. Gomez R.
Keyword(s):  
Alkaline Phosphatase ◽  
Lactate Dehydrogenase ◽  
Enzymatic Activity ◽  
Blood Urea Nitrogen ◽  
Aspartate Aminotransferase ◽  
Alanine Aminotransferase ◽  
Target Organ ◽  
Biochemical Changes ◽  
Urea Nitrogen ◽  
Biochemical Effects

Biochemical changes in the liver, kidneys and gills of rosy barbs due to toxicity of CCl4 were measured after 96 hour exposure. Alanine aminotransferase (ALT), aspartate aminotransferase (AST), alkaline phosphatase (ALP), lactate dehydrogenase (LDH), blood urea nitrogen (BUN) and creatinin (CRN), levels were measured. Significant increase in ALP, ALT, LDH and BUN activities were observed in the liver in the treated groups compared to controls (P < 0.05). AST level was significantly higher in the kidneys. This study indicates that the enzymatic activity was comparatively higher in the liver than kidneys or gills, suggesting that the liver is the target organ of CCL4 toxicity to rosy barbs.Keywords: Toxicity, Rosy Barb, CCl4doi:10.3126/on.v3i1.330Our Nature (2005)5:20-25

scholarly journals Comparison of a full-spectrum multi-analyte clinical analyser with six reference instruments using canine and feline blood samples

2017 ◽  
Vol 62 (No. 6) ◽  
pp. 342-350
Author(s):  
CS Lin ◽  
GH Chiang ◽  
CH Liu ◽  
HC Tsai ◽  
CC Yang ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Bile Acid ◽  
Blood Urea Nitrogen ◽  
Total Protein ◽  
Aspartate Aminotransferase ◽  
Alanine Aminotransferase ◽  
Total Bilirubin ◽  
Total Bile Acid ◽  
Analytical Performance ◽  
Blood Samples

In this study, we report the characterisation of a novel centrifugation and spectrum-integrated veterinary clinical analyser, the AmiShield<sup>TM</sup>, which has been developed for the multiplex measurement of biochemical, electrolyte and immunoassay parameters in a point-of-care testing environment. The aims of this study were to evaluate the analytical performance of the AmiShield<sup>TM</sup> and to compare it with six reference instruments using clinical blood samples. Two hundred and four canine and 120 feline blood samples collected from veterinary teaching hospitals were analysed in parallel using the AmiShield and appropriate reference instruments. All results were evaluated separately for canine and feline specimens. The instrument’s analytical performance was evaluated initially for short- and long-term precision, bias, and observed total error using quality control material. This was followed by comparison of clinical specimens on the AmiShield analyser in parallel with the Vitros and Hitachi for biochemical parameters, VetScan and SNAPshot for total bile acids, and VetLyte and Biolyte for electrolytes. Overall, the AmiShield analyser’s performance met the standards of the American Society for Veterinary Clinical Pathology for total allowable error for most analytes, and can be considered suitable for use in veterinary clinical practices. Using canine samples, excellent correlation coefficients (r ≧ 0.92) were identified for 14 analytes of various categories including glucose, total protein, aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, total bilirubin, amylase, blood urea nitrogen, creatinine, phosphorus, Na<sup>+</sup>, K<sup>+</sup>, Cl<sup>–</sup> and total bile acid, while good correlations (0.91 ≧ r ≧ 0.80) were recorded for albumin (r = 0.91). Bland-Altman difference plots also showed agreement (greater than 95% within Limits of Agreement) for glucose, total protein, albumin, alanine aminotransferase, alkaline phosphatase, total bilirubin, amylase, blood urea nitrogen, creatinine, Na<sup>+</sup>, K<sup>+</sup>, Cl<sup>–</sup> and total bile acid between AmiShield and the reference instruments. However, aspartate aminotransferase and phosphorus exhibited higher outliers, implying potential problems associated with matrix interferences such as lipemic samples, which warrant further study. This study demonstrates that the AmiShield compares favourably with standard reference instruments, and the new device generated data of high quality for most analytes in clinical canine and feline samples. The capability of reliably measuring multi-category analytes in one device using minute amounts (170 μl) of whole blood and short turn-around times (&lt; 15 min) underlines the high potential of the device as a good alternative in-house diagnostic application.

Hepatotoxicity Associated with Cisplatin Chemotherapy

1993 ◽  
Vol 27 (4) ◽  
pp. 438-441 ◽  
Author(s):  
Robert J. Cersosimo
Keyword(s):  
Squamous Cell Carcinoma ◽  
Alkaline Phosphatase ◽  
Lactate Dehydrogenase ◽  
Cell Carcinoma ◽  
Liver Damage ◽  
Aspartate Aminotransferase ◽  
Alanine Aminotransferase ◽  
Case Reports ◽  
Normal Limits ◽  
Case Summary

OBJECTIVE: To report a case of possible cisplatin-associated hepatotoxicity. CASE SUMMARY: A 69-year-old man received three cycles of cisplatin (100 mg/m2) and fluorouracil (1000 mg/m2/d for five days) for management of squamous cell carcinoma of the head and neck. Liver enzyme concentrations were within normal limits prior to each cycle of therapy but the aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, and lactate dehydrogenase concentrations increased on the second day of each cycle. The concentrations began to decline on day 3 of each course, despite continued fluorouracil administration, and returned to normal by day 10. The patient's antiemetic therapy included metoclopramide in cycle 1 and ondansetron in cycles 2 and 3, which may have contributed to the enzyme elevations. DISCUSSION: Case reports of cisplatin-associated hepatotoxicity are reviewed. An association between cisplatin administration and hepatotoxicity is proposed in this patient. CONCLUSIONS: This patient may have experienced cisplatin-induced liver damage. Metoclopramide and ondansetron may have contributed to this effect.

Production and certification of secondary enzyme reference materials (ERMs). Part 1: Preparation of the sera and some of their properties.

1986 ◽  
Vol 32 (10) ◽  
pp. 1901-1905 ◽  
Author(s):  
J C Koedam ◽  
G M Steentjes ◽  
S Buitenhuis ◽  
E Schmidt ◽  
R Klauke
Keyword(s):  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Reference Material ◽  
Human Serum ◽  
Dehydrogenase Activity ◽  
Aspartate Aminotransferase ◽  
Alanine Aminotransferase ◽  
Glutamate Dehydrogenase Activity ◽  
The Stability ◽  
Clinical Enzymology

Abstract We produced three batches of a human-serum-based enzyme reference material (ERM) enriched with human aspartate aminotransferase (EC 2.6.1.1), alanine aminotransferase (EC 2.6.1.2), creatine kinase (EC 2.7.3.2), and lactate dehydrogenase (EC 1.1.1.27). The added enzymes were not exhaustively purified; thus the final ERMs contained some enzymes as contaminants, of which only glutamate dehydrogenase activity might interfere. The stability during storage and after reconstitution was good. The commutability of the four enzymes in the three ERM batches was also good, except when German or Scandinavian methods for aminotransferases were involved. The temperature-conversion factors for the ERMs were equivalent to those for patients' sera. Reactivation after reconstitution was complete within 5 min and was independent of the temperature of the reconstitution fluid. We believe that these secondary ERMs will aid in the transfer of accuracy between well-defined reference methods and daily working methods so that clinical enzymology results will become more comparable from laboratory to laboratory.

Hepatotoxic effects of chloroform extract of Artemisia macivera Linn in rats following intraperitoneal administration of different subchronic doses

2010 ◽  
Vol 30 (1) ◽  
pp. 25-33 ◽  
Author(s):  
SE Atawodi ◽  
AC Ene ◽  
DA Ameh
Keyword(s):  
Alkaline Phosphatase ◽  
Total Protein ◽  
Aspartate Aminotransferase ◽  
Alanine Aminotransferase ◽  
Intraperitoneal Administration ◽  
Chloroform Extract ◽  
Hepatic Tissue ◽  
Albino Rats ◽  
High Dose ◽  
Hepatocellular Injury

The possible hepatotoxic effects of chloroform extract of Artemisia maciverae was evaluated biochemically and histologically using male Swiss albino rats, randomly assigned into four groups of 24 animals each. The groups (control, 50, 100 and 200 mg/kg body weight) were treated for 60 days and then monitored for another 30 days before sacrifice. Alanine aminotransferase, aspartate aminotransferase, alkaline phosphatase, bilirubin (total and direct), total protein and albumin were assessed colorimetrically, while tissue specimens were subjected to histological examination following standard hematoxyline-eosin staining techniques. After 1 week of treatment, the extract caused statistically significant elevation in levels of serum alanine aminotransferase, aspartate aminotransferase, alkaline phosphatase and bilirubin (total and direct), while there was significant (p < 0.05) decrease in the levels of serum total protein and albumin at the onset of treatment when compared with the control. These abnormalities in the levels of serum biochemical parameters were spontaneously corrected within 2 weeks of treatment. Similarly, histological assessment showed severe hepatic tissue injuries after 1 week, but these organs recovered spontaneously by the second week of treatment. The results indicate that long-term exposure to therapeutic doses of chloroform extract of A maciverae is relatively safe, but high dose exposure may result in hepatocellular injury.

scholarly journals Analysis of enzyme activity and the level of malondialdehyde in the saliva of children with gingivitis

2009 ◽  
Vol 66 (11) ◽  
pp. 892-896
Author(s):  
Olivera Trickovic-Janjic ◽  
Tatjana Cvetkovic ◽  
Mirjana Apostolovic ◽  
Draginja Kojovic ◽  
Ljiljana Kostadinovic ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Aspartate Aminotransferase ◽  
Alanine Aminotransferase ◽  
Study Groups ◽  
Functional Condition ◽  
Gamma Glutamyl Transferase ◽  
Gamma Glutamyl ◽  
Severe Inflammation ◽  
Glutamyl Transferase

Introduction/Aim. By analyzing activity of some of the enzymes normally present in the saliva and the level of malondialdehyde in gingivitis, it is possible to estimate the functional condition of parodontium, and the examined parameters can be considered as biochemical markers of its functional condition. The aim of this paper was to examine activity of alanine aminotransferase, aspartate aminotransferase, gamma glutamyl transferase, lactate dehydrogenase and the level of malondialdehyde in the saliva of children affected with gingivitis, as well as the values of the mentioned parameters in relation to the level of the inflammation of gingiva. Methods. The research included 120 children at the age of 12.2 with permanent dentition. L?e and Silness gingival index was used to estimate the condition of gingiva, based on which the children were classified into four groups: the children with healthy gingiva (the control groups), the children with mild, moderate and severe inflammation of gingiva (the study group). Enzymes of the saliva were determined by the use of original tests and measured by the autoanalyser (Bio Systems A25, Spain). A modified method with tiobarbituric acid was used to determine malondialdehyde in nonstimulated mixed saliva. Results. The results of the examined enzyme activity and the level of malondialdehyde in the saliva of the study groups showed statistically considerably higher values for the level of malondialdehyde (p < 0.001), for the activity of aspartate aminotransferase and gamma glutamyl transferase (p < 0.01), as well as for alanine aminotransferase (p < 0.05) in comparison with the control group, whereas the activity of lactate dehydrogenase did not show a statistically significant increase. In relation to the level of the inflammation of gingiva, the results of the examination of the enzyme activity in the study groups showed statistically significantly higher values in the group with severe inflammation in comparison with those with mild, as well as the moderate inflammatory, except for the gamma glutamyl transferase, and in the group with moderate inflammation compared to that with the mild one, except for alanine aminotransferase. The results of the examination of the level of malondialdehyde in the saliva of the study groups did not show a statistically significantly increase in relation to the level of the inflammation of gingiva. Conclusion. There is a higher level of alanine aminotransferase, aspartate aminotransferase, gamma glutamyl transferase and lactate dehydrogenase enzyme activity together with the higher level of malondialdehyde in the saliva of children with gingivitis in comparison with the activity of the same enzymes and the level of malondialdehyde in the saliva of children without gingivitis. The activity of the examined enzymes in the saliva of children with gingivitis increases in relation to the intensity of the pathological process, whereas the level of malondialdehyde shows no significant difference in relation to the level of the inflammation of gingiva.

scholarly journals Blood Biomarkers of Recovery Efficiency in Soccer Players

2019 ◽  
Vol 16 (18) ◽  
pp. 3279 ◽  
Author(s):  
Anna Nowakowska ◽  
Dorota Kostrzewa-Nowak ◽  
Rafał Buryta ◽  
Robert Nowak
Keyword(s):  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Alanine Aminotransferase ◽  
Soccer Players ◽  
Control Group ◽  
Iron Level ◽  
Recovery Efficiency ◽  
Lactate Dehydrogenase Activity ◽  
Over Time

Physical exercise strongly affects human metabolism and causes biochemical changes. This study aimed to investigate the relationship between routine plasma biomarker levels and recovery efficiency in soccer players during an entire competitive match season. The players participating in the study were divided into a midfielder/defender group (seven midfielders and seven defenders) and a goalie/substitute group (six persons—goalkeepers and players with a short cumulative match-time). The fasting capillary blood samples were taken 17–24 h after each competitive match. The blood plasma was used to determine the creatinine, urea, alkaline phosphatase, creatine kinase, lactate dehydrogenase, aspartate and alanine aminotransferase, iron and magnesium levels of the athletes. The levels of (AST) (aspartate aminotransferase), (ALT) (alanine aminotransferase) and (Cr) creatinine were higher in the midfielder/defender group than in the control group, but only AST and Cr significantly varied over time (AST decreased, and Cr increased with time). The (LDH) (lactate dehydrogenase) activity and urea level were significantly lower in the midfielder/defender group than in the goalie/substitute group, and it significantly varied over time (LDH decreased, and urea increased with time). No differences in the (CK) creatine kinase and (ALP) alkaline phosphatase activities between the groups was found, although CK increased significantly with time in the midfielder/defender group (particularly midfielders in the spring round). In midfielders, the AST activity and the iron level were significantly lower in the spring than in the autumn round. On the contrary, ALT, CK, urea and magnesium levels were significantly higher in the spring than in autumn round. A long-term measurement of biochemical parameters in elite soccer players indicated that AST, CK, LDH and creatinine levels, when analyzed together, could constitute a useful set of markers for monitoring recovery periods.

scholarly journals Effect of Various Diluents on the Activity of Several Enzymes Present in Serum

1973 ◽  
Vol 19 (9) ◽  
pp. 1079-1080
Author(s):  
Ted W Fendley ◽  
Jane M Hochholzer ◽  
Christopher S Frings
Keyword(s):  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Confidence Level ◽  
Aspartate Aminotransferase ◽  
Nacl Solution ◽  
Manual Method ◽  
Accuracy And Precision ◽  
Significant Difference

Abstract We have evaluated the effect of diluting serum with water or NaCl solution (8.5 or 9.0 g/liter) before assaying by a manual method for creatine kinase (EC 2.7.3.2), alkaline phosphatase (EC 3.1.3.1), lactate dehydrogenase (EC 1.1.1.27), and aspartate aminotransferase (EC 2.6.1.1) activity. The t test and the F test show no significant difference in the accuracy and precision of the assays at the 95% confidence level when 100 different samples were compared for each enzyme activity after use of the three diluents.

scholarly journals Standards versus Standardised Methods in Enzyme Assay

1983 ◽  
Vol 20 (1) ◽  
pp. 52-59 ◽  
Author(s):  
R T P Jansen ◽  
A P Jansen
Keyword(s):  
Quality Control ◽  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Alanine Aminotransferase ◽  
Enzyme Assay ◽  
Control Program ◽  
Internal Quality ◽  
Quality Control Program ◽  
Control Serum

In a trial of the Netherlands coupled external/internal quality control program a control serum and an enzyme standard were analysed over a period of eight weeks, five times each week. Five enzymes were determined: alkaline phosphatase, creatine kinase, lactate dehydrogenase, alanine aminotransferase, and γ-glutamyltransferase. The measured values in the serum were converted to the standards. Those laboratories using the recommended methods also submitted their non-transformed serum values. The following standardisation techniques have been compared: ( a) no standardisation of methodology but use of enzyme standards; ( b) standardisation of methodology; ( c) standardisation of methodology combined with use of an enzyme standard. Results were submitted to analysis of variance. Standardisation of methodology did not yield smaller interlaboratory variation than the standardisation with enzyme standards. In this trial a combination of both standardisation techniques yielded generally better results. Results for γ-glutamyltransferase indicate that standardisation of substrate may be necessary apart from the use of an enzyme standard. The preparation of stable enzyme standards is stressed.

Sign in / Sign up

Export Citation Format

Share Document