Stabilities of some constituents of marmoset (Callithrix jacchus) plasma under various conditions of storage.

Abstract The stability of various marmoset (Callithrix jacchus) plasma constituents was investigated after storage at room temperature, 4 degrees C, and -20 degrees C. The method of sequential analysis ensured that the between-run bias of the methods of analysis used was drastically reduced, and the definitions of stability were linked to the imprecision of these methods. Optimal conditions for storage for as long as 48 h depended on the analyte being measured. Room temperature was optimal for cholinesterase and acetylcholinesterase; 4 degrees C for protein, albumin, alanine aminotransferase, isocitrate dehydrogenase, sorbitol dehydrogenase, lactate dehydrogenase, and glutamate dehydrogenase; and -20 degrees C for glutathione reductase and alkaline phosphatase. For aspartate amino-transferase and gamma-glutamyltransferase, either 4 degrees C or -20 degrees C would be suitable. Reasons are advanced for some conflicting reports in the published work, and we emphasize the need to investigate each analyte and species separately.

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

Clinical Chemistry ◽

10.1093/clinchem/32.10.1901 ◽

1986 ◽

Vol 32 (10) ◽

pp. 1901-1905 ◽

Cited By ~ 6

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.

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Automated Measurement of Lactate Dehydrogenase, Alkaline Phosphatase and Gamma-Glutamyltransferase in Urines: An Alternative to the Manual Procedure

Enzyme ◽

10.1159/000468793 ◽

1992 ◽

Vol 46 (4-5) ◽

pp. 234-238 ◽

Cited By ~ 1

Author(s):

Elena Matteucci ◽

Luisa Pellegrini ◽

Christina Uncini-Manganelli ◽

Renzo Navalesi ◽

Ottavio Giampietro

Keyword(s):

Alkaline Phosphatase ◽

Lactate Dehydrogenase ◽

Automated Measurement ◽

Gamma Glutamyltransferase

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Blood Biomarkers of Recovery Efficiency in Soccer Players

International Journal of Environmental Research and Public Health ◽

10.3390/ijerph16183279 ◽

2019 ◽

Vol 16 (18) ◽

pp. 3279 ◽

Cited By ~ 5

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.

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The EPOS Automated Selective Chemistry Analyzer evaluated.

Clinical Chemistry ◽

10.1093/clinchem/32.1.165 ◽

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.

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

Our Nature ◽

10.3126/on.v3i1.330 ◽

1970 ◽

Vol 3 (1) ◽

pp. 20-25 ◽

Cited By ~ 11

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

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Standards versus Standardised Methods in Enzyme Assay

Annals of Clinical Biochemistry International Journal of Laboratory Medicine ◽

10.1177/000456328302000108 ◽

1983 ◽

Vol 20 (1) ◽

pp. 52-59 ◽

Cited By ~ 15

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.

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Comparison of some biochemical and mineral indices among Norik breed Muráň Plain type and Hucul breed mares

Acta Veterinaria Brno ◽

10.2754/avb201584020113 ◽

2015 ◽

Vol 84 (2) ◽

pp. 113-117 ◽

Cited By ~ 2

Author(s):

Ján Pošivák ◽

Eva Styková ◽

František Novotný ◽

Igor Valocký ◽

Jana Noskovičová ◽

...

Keyword(s):

Alkaline Phosphatase ◽

Lactate Dehydrogenase ◽

Aspartate Aminotransferase ◽

Biochemical Analysis ◽

Iron Chloride ◽

Parasitic Diseases ◽

Gamma Glutamyltransferase ◽

Significant Difference ◽

Mineral Profile ◽

Biochemical Indices

Biochemical analysis in horses is an important aid for determining correct clinical diagnosis of general, infectious, and some parasitic diseases. This work studied the biochemical and mineral indices in mares of two breeds: the Norik breed Muráň Plain type and the Hucul breed. A total of 34 mares of the Norik breed Muráň Plain type (aged 15.18 ± 5.99 years) and 28 Hucul mares (aged 9.03 ± 5.50 years) were used. Blood serum was analysed using the biochemical analyser Cobas c111 (Roche, Switzerland). Significant difference (P < 0.05) was found between the Norik breed Muráň Plain type and the Hucul mares in aspartate aminotransferase, alkaline phosphatase, lactate dehydrogenase and gamma-glutamyltransferase activity; significant difference (P < 0.01) was found in urea values; and highly significant difference (P < 0.001) was found in glucose values. The mineral profile elements showed a highly significant differences (P < 0.001) between the Norik breed Muráň Plain type and the Hucul mares in phosphorus, magnesium, iron, chloride, potassium, and sodium concentrations. The results confirmed that there are significant differences between horse breeds in some biochemical indices. Therefore, it is appropriate to determine reference values for other horse breeds, as well. To our knowledge, this is the first report that compares biochemical and mineral indices between the Norik breed Muráň Plain type and the Hucul breed.

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Hepatotoxicity Associated with Cisplatin Chemotherapy

Annals of Pharmacotherapy ◽

10.1177/106002809302700408 ◽

1993 ◽

Vol 27 (4) ◽

pp. 438-441 ◽

Cited By ~ 42

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.

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Normal limits of urinary excretion of eleven enzymes.

Clinical Chemistry ◽

10.1093/clinchem/22.10.1567 ◽

1976 ◽

Vol 22 (10) ◽

pp. 1567-1574 ◽

Cited By ~ 51

Author(s):

D Maruhn ◽

I Fuchs ◽

G Mues ◽

K D Bock

Keyword(s):

Alkaline Phosphatase ◽

Lactate Dehydrogenase ◽

Urinary Excretion ◽

Gel Filtration ◽

Reference Intervals ◽

Creatinine Concentration ◽

Urinary Creatinine ◽

Gamma Glutamyltransferase ◽

Normal Limits ◽

Alpha Glucosidase

Abstract Urinary excretion of lactate dehydrogenase, hydroxybutyrate dehydrogenase, gamma-glutamyltransferase, alkaline phosphatase, arylsulphatase A, alpha-glucosidase, beta-galactosidase, trehalase, N-acetyl-beta-glucosaminidase, beta-glucuronidase, and leucinearylamidase was studies in a carefully selected group of 100 healthy subjects, 50 women and 50 men. Enzyme activities were assayed in 3-h morning samples after gel filtration of the urine. Activities were related to time volume, and to urinary creatinine concentration. Several transforming functions had to be applied to enzyme output data to obtain an approximation to gaussian frequency distribution. Men showed a significantly higher excretion of gamma-glutamyltransferase, alpha-glucosidase, trehalase, N-acetyl-beta-glucosaminidase,beta-glucuronidase, and leucine arylamidase activity than did women if enzyme activity was related to urinary time volume. Women excreted more lactate dehydrogenase, hydroxybutyrate dehydrogenase, gamma-glutamyltransferase, alkaline phosphatase, alpha-glucosidase, trehalase, and N-acetyl-beta-glucosaminidase activity than did men, if urinary creatinine was used as the basis of reference. Reference intervals were calculated as 2.5 and 97.5 percentiles for both sexes.

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