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 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.

Hepatic infarction: biochemical study of a case.

1983 ◽  
Vol 29 (10) ◽  
pp. 1850-1851 ◽  
Author(s):  
G N Hoag ◽  
T P Orr ◽  
D R Amies
Keyword(s):  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Biochemical Study ◽  
Post Mortem ◽  
Lactate Dehydrogenase Activity ◽  
Gamma Glutamyltransferase ◽  
Hepatocellular Necrosis ◽  
Hepatic Infarction ◽  
Muscle Breakdown

Abstract Hepatic infarction was observed post mortem in a 27-year-old man who died of aortic dissection. Blood had been sampled at admission and 12 and 19 hours later. Values for aspartate aminotransferase and alanine aminotransferase in serum were markedly above normal, whereas those for alkaline phosphatase and gamma-glutamyltransferase were only marginally increased. A threefold-increased creatine kinase was ascribable solely to isoenzyme CK-3, suggesting muscle breakdown. Moreover, total lactate dehydrogenase activity was increased threefold, accounted for by a ninefold increase in LD-5 isoenzyme. Those enzyme activities in serum that evidently are associated with acute hepatocellular necrosis increase quickly in hepatic infarction, and CK isoenzyme assay is a useful adjunct if LD-5 increases are significant.

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.

Improved column method for separating lactate dehydrogenase isoenzymes 1 and 2.

1978 ◽  
Vol 24 (3) ◽  
pp. 480-482 ◽  
Author(s):  
D W Mercer
Keyword(s):  
Myocardial Infarction ◽  
Acute Myocardial Infarction ◽  
Creatine Kinase ◽  
Heart Disease ◽  
Lactate Dehydrogenase ◽  
Sodium Chloride ◽  
Lactate Dehydrogenase Activity ◽  
Column Method ◽  
Creatine Kinase Mb ◽  
Lactate Dehydrogenase Isoenzymes

Abstract Lactate dehydrogenase (LD) isoenzymes 1 and 2 in human serum were separated on a column of diethylaminoethyl-Sephadex. Samples layered on mini-columns were eluted with buffered sodium chloride (100, 150, and 200 mmol/liter). Lactate dehydrogenase activity in column effluents was measured by the Wacker method, and their isoenzyme content was evaluated by electrophoresis on polyacrylamide gel. Results for column-fractionated LD-1 and LD-2 were expressed in two ways: LD-1/LD-2 ratios and total LD-1 + LD-2 activities. The former is a more specific indicator of myocardial infarction than the latter. Sera from 10 patients with acute myocardial infarction (increased creatine kinease isoenzyme MB activity) exhibited ratios in the range of 0.92 to 1.56, ratios for 10 patients without heart disease (normal creatine kinase MB) ranged from 0.33 to 0.69.

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.

Effect of Lactate Dehydrogenase Isoenzymes on the Coupled Enzymatic Assay for Alanine Aminotransferase Activity

1975 ◽  
Vol 21 (3) ◽  
pp. 330-333 ◽  
Author(s):  
Michael M Chang ◽  
Tai Wha Chung
Keyword(s):  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Alanine Aminotransferase ◽  
Rabbit Muscle ◽  
Aminotransferase Activity ◽  
Lactate Dehydrogenase Activity ◽  
Enzymatic Assays ◽  
Substrate Specificities ◽  
Lactate Dehydrogenase Isoenzymes ◽  
Alanine Aminotransferase Activity

Abstract We show an example of the importance of specifying the form of isoenzyme and source of indicator enzymes to be used in coupled enzymatic assays. When we compared H4 (pig heart) and M4 (rabbit muscle) isoenzymes of lactate dehydrogenase for their suitability as indicator enzymes in the assay for alanine aminotransferase activity, we found that about fourfold as much M4 as H4 was required in terms of lactate dehydrogenase activity to reflect accurately equivalent amounts of alanine aminotransferase activity. Moreover, the substrate specificities of the two isoenzymes differed quantitatively.

The EPOS Automated Selective Chemistry Analyzer evaluated.

1986 ◽  
Vol 32 (1) ◽  
pp. 165-169
Author(s):  
G C Moses ◽  
G O Lightle ◽  
J F Tuckerman ◽  
A R Henderson
Keyword(s):  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Data Reduction ◽  
Analytical Performance ◽  
Gamma Glutamyltransferase ◽  
External Data ◽  
Reduction System ◽  
Oriented System

Abstract We evaluated the analytical performance of the EPOS (Eppendorf Patient Oriented System) Automated Selective Chemistry Analyzer, using the following tests for serum analytes: alanine and aspartate aminotransferases, lactate dehydrogenase, creatine kinase, gamma-glutamyltransferase, alkaline phosphatase, and glucose. Results from the EPOS correlated well with those from comparison instruments (r greater than or equal to 0.990). Precision and linearity limits were excellent for all tests; linearity of the optical and pipetting systems was satisfactory. Reagent carryover was negligible. Sample-to-sample carryover was less than 1% for all tests, but only lactate dehydrogenase was less than the manufacturer's specified 0.5%. Volumes aspirated and dispensed by the sample and reagent II pipetting systems differed significantly from preset values, especially at lower settings; the reagent I system was satisfactory at all volumes tested. Minimal daily maintenance and an external data-reduction system make the EPOS a practical alternative to other bench-top chemistry analyzers.

Electronic Correction of Values That Are "Off-Scale" in the "SMA-6" System for Continuous-flow Analysis

1975 ◽  
Vol 21 (1) ◽  
pp. 151-154
Author(s):  
Louis Rosenfeld
Keyword(s):  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Continuous Flow ◽  
Chloride Solution ◽  
Sodium Chloride Solution ◽  
Electronic Device ◽  
Flow Analysis ◽  
Continuous Flow Analysis ◽  
Chart Paper

Abstract Data are presented for an electronic device that automatically halves "off-scale" signal voltages on the "SMA Flex-6" System (Technicon). This extends the usefulness of the system by obviating the need for most repeat analyses on dilutions of specimens containing constituents in concentrations that exceed the limits of the pre-calibrated chart paper. Accurate results are obtained because the chemical reactions are shown to be linear up to nearly twice the maximum calibration on the recorder paper for the following analytes: bilirubin, total and direct (20.0 mg/dl); alkaline phosphatase (700 U/ liter); lactate dehydrogenase (1200 U/liter); creatine kinase (2400 U/liter); and aspartate aminotransferase (600 U/liter). In contrast, dilution of sera 2-, 5-, and 10-fold with sodium chloride solution (8.5 g/liter) produces positive errors ranging from 6 to 38% for these enzymes, but has no significant effect on bilirubin.

Hepatic stem cells and their enzymatic markers- A review

2018 ◽  
Author(s):  
Amit Kumar ◽  
Sourabh Sulabh
Keyword(s):  
Stem Cells ◽  
Alkaline Phosphatase ◽  
Lactate Dehydrogenase ◽  
Progenitor Cells ◽  
Ethical Issues ◽  
Fetal Liver ◽  
Lactate Dehydrogenase Activity ◽  
Liver Stem Cells ◽  
Enzymatic Markers

Stem cells are those cells which show capacity for self-renewal and ability to give rise to multiple differentiated cellular populations. Enzymatic activity, as a marker for cell proliferation and cell viability, is used by metabolic activity assays. Liver stem cells/progenitor cells can be a useful source of liver treatment. They can repopulate and restore injured liver. Fetal liver stem/ progenitor cells have been found to be more capable in this, but are subjected to ethical issues. Adult liver stem cells and stem cells from animals can be used. Alkaline phosphatase and lactate dehydrogenase are enzymatic markers of in vitro hepatocyte culture. During in vitro cell culture, in the culture medium, secreted alkaline phosphatase activity increases during exponential growth of cells, whereas low extracellular lactate dehydrogenase activity indicates increased number of viable cells. Alkaline phosphatase and lactate dehydrogenase activities can be used to assess hepatocytes proliferation in vitro.

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