Gamma-Glutamyltransferase as a Marker for the Pasteurization of Raw Milk

1998 ◽  
Vol 61 (8) ◽  
pp. 1057-1059 ◽  
Author(s):  
FILOMENA DOS ANJOS ◽  
ADELINA MACHADO ◽  
CRISTINA FERRO ◽  
FRANK OTTO ◽  
EITAN BOGIN
Keyword(s):  
Alkaline Phosphatase ◽  
Lactate Dehydrogenase ◽  
Heat Resistance ◽  
Raw Milk ◽  
Heat Inactivation ◽  
Gamma Glutamyltransferase ◽  
Complete Inactivation ◽  
Heat Treated ◽  
Commercial Kits ◽  
Raw Cow’S Milk

The degree and rate of inactivation of gamma-glutamyltransferase in raw cow's milk by heating at 50, 60,70, and 80°C for 1, 2, 3, 5, 10, 15, 20, 25, and 30 min were measured to evaluate the suitability of this enzyme as a marker for the pasteurization of milk. The enzymes alkaline phosphatase and lactate dehydrogenase were also measured under similar conditions for comparison. The patterns of heat inactivation of gamma-glutamyltransferase and alkaline phosphatase were similar, with only a minimal inactivation of the enzymes at 50°C. The rate of inactivation increased as a result of increasing temperatures and time. A complete inactivation of both enzymes was seen at 70°C after 10 min and at 80°C after 1 min. Lactate dehydrogenase showed a higher heat resistance with almost complete inactivation at 70°C for 30 min, and compete inactivation at 80°C for 3 min. No activities of these enzymes were found in commercially pasteurized or heat-treated milk. The levels of gamma-glutamyltransferase in raw milk were between 8 and 10% higher than those of alkaline phosphatase and lactate dehydrogenase, making it more sensitive and accurate as a testing marker. It seems that gamma-glutamyltransferase may serve as a good pasteurization marker. Furthermore, the simplicity of testing and the availability of commercial kits for testing by both wet and dry chemistry make it an attractive choice, especially because dry chemistry procedures overcome the difficulties originating from the turbidity of milk, which interferes with spectrophotometric procedures.

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

Enzyme ◽  
1992 ◽  
Vol 46 (4-5) ◽  
pp. 234-238 ◽  
Author(s):  
Elena Matteucci ◽  
Luisa Pellegrini ◽  
Christina Uncini-Manganelli ◽  
Renzo Navalesi ◽  
Ottavio Giampietro
Keyword(s):  
Alkaline Phosphatase ◽  
Lactate Dehydrogenase ◽  
Automated Measurement ◽  
Gamma Glutamyltransferase

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.

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

2015 ◽  
Vol 84 (2) ◽  
pp. 113-117 ◽  
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.

Normal limits of urinary excretion of eleven enzymes.

1976 ◽  
Vol 22 (10) ◽  
pp. 1567-1574 ◽  
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.

scholarly journals Suppression of Food Allergic Symptoms by Raw Cow’s Milk in Mice is Retained after Skimming but Abolished after Heating the Milk—A Promising Contribution of Alkaline Phosphatase

Nutrients ◽  
2019 ◽  
Vol 11 (7) ◽  
pp. 1499 ◽  
Author(s):  
Suzanne Abbring ◽  
Joseph Thomas Ryan ◽  
Mara A.P. Diks ◽  
Gert Hols ◽  
Johan Garssen ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Protective Effect ◽  
Raw Milk ◽  
Fat Content ◽  
Cow’S Milk ◽  
Protective Effects ◽  
Pasteurized Milk ◽  
Cow's Milk ◽  
Allergic Symptoms ◽  
Raw Cow’S Milk

Raw cow’s milk was previously shown to suppress allergic symptoms in a murine model for food allergy. In the present study, we investigated the contribution of fat content and heat-sensitive milk components to this allergy-protective effect. In addition, we determined the potency of alkaline phosphatase (ALP), a heat-sensitive raw milk component, to affect the allergic response. C3H/HeOuJ mice were treated with raw milk, pasteurized milk, skimmed raw milk, pasteurized milk spiked with ALP, or phosphate-buffered saline for eight days prior to sensitization and challenge with ovalbumin (OVA). Effects of these milk types on the allergic response were subsequently assessed. Similar to raw milk, skimmed raw milk suppressed food allergic symptoms, demonstrated by a reduced acute allergic skin response and low levels of OVA-specific IgE and Th2-related cytokines. This protective effect was accompanied by an induction of CD103+CD11b+ dendritic cells and TGF-β-producing regulatory T cells in the mesenteric lymph nodes. Pasteurized milk was not protective but adding ALP restored the allergy-protective effect. Not the fat content, but the heat-sensitive components are responsible for the allergy-protective effects of raw cow’s milk. Adding ALP to heat-treated milk might be an interesting alternative to raw cow’s milk consumption, as spiking pasteurized milk with ALP restored the protective effects.

Chemical and clinical evaluation of the random access analyzer "RA-1000".

1984 ◽  
Vol 30 (3) ◽  
pp. 364-368 ◽  
Author(s):  
M K Schwartz ◽  
B E Statland ◽  
J Coughlin ◽  
C Eisen ◽  
M Fleisher ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Total Protein ◽  
Random Access ◽  
Inorganic Phosphorus ◽  
Production Model ◽  
Excellent Correlation ◽  
Gamma Glutamyltransferase

Abstract In the RA-1000, a random-access discrete analyzer, an inert fluorocarbon fluid is used to prevent interaction and carryover. Production-model instruments were evaluated in two laboratories with respect to determination of glucose, creatinine, total protein, inorganic phosphorus, cholesterol, alkaline phosphatase, lactate dehydrogenase, creatine kinase, gamma-glutamyltransferase, and aspartate and alanine aminotransferases. Within-run, among-run, and day-to-day (for 15 days) precision was assessed, and results were correlated with those obtained by the methods routinely in use in our departments. Precision was excellent, correlation acceptable.

Effect of Sporulation Media on the Heat Resistance of Bacillus stearothermophilus Spores1

1977 ◽  
Vol 40 (4) ◽  
pp. 232-233 ◽  
Author(s):  
J. L. MAYOU ◽  
J. J. JEZESKI
Keyword(s):  
Heat Resistance ◽  
Bacillus Stearothermophilus ◽  
Nutrient Broth ◽  
Nutrient Agar ◽  
Heat Inactivation ◽  
Vegetative Cells ◽  
Temperature Range ◽  
Heat Treated ◽  
D Values

Based on D values obtained over the temperature range of 121.1 C (250 F) to 126.7 C (260 F), Bacillus stearothermophilus vegetative cells sporulated in the presence of milk were more resistant to heat inactivation than spores grown on nutrient agar fortified with MnSo4. Spores grown in the presence of milk and heat-treated at 121.1 and 126.7 C had D values of 4.7 and 0.8 min, respectively. Spores grown on fortified nutrient agar and beat-treated at 121.1 and 126.7 C had D values of 3. 7 and 0.55 min, respectively. No difference in heat resistance was observed between spores derived from vegetative cells grown in milk or nutrient broth when tested at 121.1 C.

Measurement of six enzymes with the Kodak DTSC Module, a physician's office analyzer.

1987 ◽  
Vol 33 (10) ◽  
pp. 1911-1913 ◽  
Author(s):  
R H Ng ◽  
M Altaffer ◽  
M O'Neill ◽  
H Mukadam ◽  
B E Statland
Keyword(s):  
Quality Control ◽  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Multilayer Film ◽  
Clinical Use ◽  
Gamma Glutamyltransferase ◽  
Quality Control Materials ◽  
Interference Studies

Abstract We evaluated the performance of the Kodak DTSC Module for determination of alanine aminotransferase (ALT; EC 2.6.1.2), aspartate aminotransferase (2.5.1.2), alkaline phosphatase (3.1.3.1), creatine kinase (2.7.3.2), gamma-glutamyltransferase (2.3.2.2), and lactate dehydrogenase (1.1.1.27). The DTSC is a "special chemistry" accessory for the DT60 analyzer; the same multilayer film technology as that of the Ektachem 700 is used. The overall precision, assessed over a three-month period with two serum-based quality control materials, ranged from 2.2 to 8.0%. DTSC results for patients' specimens correlated well with those by the Technicon RA-1000 analyzer. The performance of the analyzer in linearity and interference studies was satisfactory for clinical use. The DTSC is simple to operate and has no technique-dependent step; it should be useful for the physician's office laboratory.

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

1984 ◽  
Vol 30 (1) ◽  
pp. 101-104 ◽  
Author(s):  
C W Davy ◽  
M R Jackson ◽  
J M Walker
Keyword(s):  
Alkaline Phosphatase ◽  
Lactate Dehydrogenase ◽  
Alanine Aminotransferase ◽  
Room Temperature ◽  
Sequential Analysis ◽  
Callithrix Jacchus ◽  
Optimal Conditions ◽  
Gamma Glutamyltransferase ◽  
Aspartate Amino Transferase ◽  
The Stability

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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