Analysis of the influence of copper on carbohydrate metabolism in carp

2020 ◽  
Vol 2 ◽  
pp. 162-165
Author(s):  
L. Yu. Karpenko ◽  
◽  
P. A. Polistovskaya ◽  
A. B. Balykina ◽  
◽  
...  
Keyword(s):  
Carbohydrate Metabolism ◽  
Glucose Concentration ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Copper Acetate ◽  
The Body ◽  
Toxic Effects ◽  
Control Group ◽  
Toxic Substances ◽  
Serum Amylase Activity

The article discusses some aspects of the toxic effects of copper acetate on the body of fish. Heavy metals are highly toxic to aquat-ic organisms due to their ability to accumu-late and transform within the biocenosis of the reservoir. The aim of the study was to study the indicators of carbohydrate metabo-lism in carp after exposure to various con-centrations of copper acetate. The study of the features of carbohydrate metabolism, including the intensity and direction of ex-change can be useful in assessing the re-sponse of fish to toxic effects. During the experiment, 4 groups of fish were formed - 1 control group (10 fish), 3 experimental groups – 10 fish each. Experimental groups of fish were contained in a solution of cop-per acetate (Cu(CH3COO)2) with concentra-tions of 0.01 mg/l, 0.1 mg/l, 1 mg/l (exceeding the MPC of copper for fisheries reservoirs by 10, 100 and 1000 times, re-spectively). Glucose concentration and se-rum amylase activity were studied. Glucose is necessary for supplying energy to various processes occurring inside the body,including reactions to toxic substances. Amylase, however, is an enzyme responsible for catalyzing the breakdown of complex carbohydrates. We found such changes in carbohydrate metabolism in carp as a signifi-cant increase in serum amylase activity by 6.63%, 7.9% and 19.57% when exposed to 10, 100 and 1000 MPC of copper, respec-tively, as well as a significant increase in glucose concentration by 8.54%, 20.28% and 29.7% when exposed to 10, 100 and 1000 MPC of copper, respectively, compared to the control group.

scholarly journals Effect of Selenium Supplementation on Serum Amylase, Lactate Dehydrogenase and Alkaline Phosphatase Activities in Rats Exposed to Cadmium or Lead

2015 ◽  
Vol 47 (4) ◽  
pp. 113-121
Author(s):  
B.G. Şlencu ◽  
C. Ciobanu ◽  
Carmen Solcan ◽  
Alina Anton ◽  
St. Ciobanu ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Lactate Dehydrogenase ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Selenium Supplementation ◽  
Control Group ◽  
Ldh Activity ◽  
Cadmium And Lead ◽  
Serum Amylase Activity ◽  
Induced Changes

Abstract The purpose of the study was to assess the effect of selenium supplementation on serum amylase, lactate dehydrogenase (LDH) and alkaline phosphatase (ALP) activities in rats, during subacute exposure to toxic doses of cadmium or lead through the drinking water. The experimental groups (n=6) were: Control, Se (Se+4: 0,2 mg/l), Cd (Cd+2: 150 mg/l), Pb (Pb+2: 300 mg/l), Cd+Se (Cd+2: 150 mg/l; Se+4: 0,2 mg/l) and Pb+Se (Pb+2: 300 mg/l; Se+4: 0,2 mg/l). The animals were sacrificed after 56 days. Amylase, LDH and ALP activities were determined from serum. Se and Pb treatments caused an increase in amylase and LDH activities, when compared to Control group while Cd caused an increase in amylase activity and a decrease in LDH and ALP activities. Cd+Se caused a decrease in amylase activity and an increase in LDH activity, when compared to Cd. Pb+Se caused a decrease in amylase activity in comparison to lead. Selenium supplementation alleviated cadmium or lead induced changes in serum amylase activity. Selenium, coadministered with cadmium, caused a marked increase in serum LDH activity, when compared to cadmium alone or Control group while practically it had no effect on lead induced changes in LDH activity. Cadmium and lead induced disturbances in serum ALP activity were not influenced by selenium supplementation.

An Automated, Saccharogenic Method for Determining Serum Amylase Activity

1970 ◽  
Vol 16 (12) ◽  
pp. 985-989 ◽  
Author(s):  
Wendell R O'Neal ◽  
Nathan Gochman
Keyword(s):  
Glucose Oxidase ◽  
Blood Donors ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Serum Glucose ◽  
Normal Range ◽  
Reducing Substances ◽  
Serum Amylase Activity

Abstract An automated adaptation of the Somogyi saccharogenic determination of serum amylase is described in which conventional AutoAnalyzer modules are used. Adequate sensitivity with short incubation is achieved by incorporating glucose oxidase and catalase in the substrate to destroy serum glucose during incubation. Maltose and other dialyzable oligosaccharides are measured with the alkaline copper-neocuproine reaction. A simultaneous blank run is performed to determine reducing substances other than glucose in serum. Precision studies and correlation with a manual saccharogenic method are presented. The normal range was determined from data for 49 healthy blood donors.

(Washington University case conference): acute pancreatitis, hyperlipemia, and normal amylase.

1978 ◽  
Vol 24 (5) ◽  
pp. 815-820 ◽  
Keyword(s):  
Acute Pancreatitis ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Normal Serum ◽  
Case Conference ◽  
Diagnosis And Management ◽  
Serum Amylase Activity ◽  
Washington University

Abstract This case focuses on the biochemical findings in acute pancreatitis and the role of the laboratory in the diagnosis and management of such patients. It also illustrates a major unappreciated problem in the use of amylase determinations in patients with acute pancreatitis: normal serum amylase activity in the presence of hyperlipemia.

A New Saccharogenic Micromethod for Measurement of Amylase Activity in Biological Fluids

1970 ◽  
Vol 16 (4) ◽  
pp. 300-304 ◽  
Author(s):  
Klaus Lorentz ◽  
Detlef Oltmanns
Keyword(s):  
Standard Deviation ◽  
Blood Donors ◽  
Serum Amylase ◽  
Amylase Activity ◽  
Biological Fluids ◽  
Soluble Starch ◽  
Starch Digestion ◽  
Triphenyltetrazolium Chloride ◽  
Serum Amylase Activity ◽  
Apparently Healthy

Abstract To determine serum amylase activity we have quantitatively measured the glucose and maltose hydrolyzed from soluble starch by colorimetrically measuring the reduction of colorless triphenyltetrazolium chloride to a red formazan, which is dissolved in methanol. The method is suitable for use with microsamples of all biological fluids, and is specific for the final products of starch digestion. Values found for sera from 55 apparently healthy blood donors ranged from 0.15 to 1.55 (mean, 0.83; standard deviation, ±0.4) mg of glucose per ml per h, corresponding to 7.5 to 78 Somogyi units.

Effect of Cadmium Exposure on Serum Amylase Activity in Cadmium Electroplating Workers

2006 ◽  
Vol 1 (4) ◽  
pp. 260-267 ◽  
Author(s):  
R. B. Kalahasthi ◽  
Rajmohan Hirehal Raghavendra Rao ◽  
Rajan Bagalur Krishna Murthy ◽  
M. Karuna Kumar
Keyword(s):  
Serum Amylase ◽  
Amylase Activity ◽  
Cadmium Exposure ◽  
Serum Amylase Activity

scholarly journals Modified Form of the Fibrinogen Bβ Chain (des-Gln Bβ), a Potential Long-Lived Marker of Pancreatitis

2007 ◽  
Vol 53 (12) ◽  
pp. 2105-2111 ◽  
Author(s):  
David Schmidt ◽  
Stephen O Brennan
Keyword(s):  
Plasma Sample ◽  
Serum Amylase ◽  
Peptide Mapping ◽  
Amylase Activity ◽  
Pancreatic Disease ◽  
Reversed Phase ◽  
Ionization Mass ◽  
Carboxypeptidase A ◽  
Serum Amylase Activity

Abstract Background: During an investigation of genetic variants of fibrinogen, we observed a novel form of the Bβ chain, with a mass decrease of approximately 128 Da, in one of the controls. The plasma sample originated from an individual who had experienced acute pancreatitis a week earlier but whose serum amylase activity had returned to normal. We investigated the structure of the modified fibrinogen and explored its relationship to pancreatic disease. Method: Fibrinogen was isolated from the plasma of 9 individuals with increased pancreatic amylase activity (114–1826 U/L) and presumed pancreatitis and from 6 control individuals with amylase activities <56 U/L. Fibrinogen (or fibrin) Bβ chains were isolated by reversed-phase HPLC and analyzed directly by electrospray ionization mass spectrometry. Tryptic and CNBr peptide mapping and thrombin treatment pinpointed the location of the 128-Da loss in mass. Results: The acquired fibrinogen Bβ chain modification was attributable to the loss of its C-terminal glutamine residue. Incubating purified fibrinogen with pancreatic carboxypeptidase A (CpA) produced an identical modification. The des-Gln Bβ fibrinogen accounted for >80% of the Bβ chains in 3 of the individuals with increased amylase but only approximately 5% of the Bβ chains in control samples. Conclusion: Pancreatic CpA activity is used as an index of acute pancreatic disease, but given that the circulatory half-lives of fibrinogen and CpA are approximately 4 days and only 2.5 h, respectively, measuring des-Gln Bβ fibrinogen, the in vivo product of CpA activity, could provide clinicians with retrospective evidence of disease.

Effect of nickel exposure on serum amylase activity in nickel-plating workers

2008 ◽  
Vol 90 (2) ◽  
pp. 393-400
Author(s):  
Ravi Babu Kalahasthi ◽  
Rajmohan Hirehal Raghavendra Rao ◽  
Rajan Bagalur Krishna Murthy ◽  
M. Karuna Kumar
Keyword(s):  
Serum Amylase ◽  
Amylase Activity ◽  
Nickel Plating ◽  
Nickel Exposure ◽  
Serum Amylase Activity
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