Alkaline Phosphatase, Gamma-Glutamyl Transferase, Lactate Dehydrogenase and Creatine Kinase in Bronchial Aspirate from Neoplastic and Normal Pulmonary Tissue

Enzyme ◽  
1985 ◽  
Vol 33 (2) ◽  
pp. 105-108 ◽  
Keyword(s):  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Gamma Glutamyl Transferase ◽  
Pulmonary Tissue ◽  
Gamma Glutamyl ◽  
Bronchial Aspirate ◽  
Glutamyl Transferase

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 Comparative Study of Serum Gamma Glutamyltransferase, 5’ Nucleotidase and Alkaline Phosphatase in Icteric and an-Icteric Biliary Disease Patients

2013 ◽  
Vol 12 (1) ◽  
Author(s):  
Dr. Maninder Pal Singh Gill
Keyword(s):  
Alkaline Phosphatase ◽  
Significant Rise ◽  
Control Group ◽  
P Value ◽  
Gamma Glutamyl Transferase ◽  
Biliary Disease ◽  
Gamma Glutamyl ◽  
Hepatobiliary Diseases ◽  
Glutamyl Transferase ◽  
Diagnostic Indicator

Introduction: Diagnostic enzymology plays a useful role in evaluation of various hepatobiliary diseases and numerous enzymes have been compared in different disorders. Among these, significance of Gamma Glutamyl Transferase and 5’ Nucleotidase over Alkaline Phosphatase has been stressed repeatedly, but mainly in the icteric obstructive biliary disease patients. In this study, these three enzymes were compared not only in the icteric but also the an-icteric biliary disease patients, particularly to look for elevation and significance of these enzymes in the latter group.Methods: The study was conducted on 50 biliary disease patients, who were further divided into an-icteric (32 patients) and icteric (18 patients) subgroups depending on their bilirubin levels. 50 subjects matched for age and sex with the study group were enrolled for the control group. Gamma Glutamyl Transferase, 5’Nucleotidase, Alkaline Phosphatase and bilirubin levels were evaluated in all the patients as well as the control subjects. Results: All three enzymes showed a significant rise in the icteric subgroup (p value < 0.001). However, in the an-icteric subgroup, only Gamma Glutamyl Transferase and 5’Nucleotidase showed a significant rise. The rise was more for Gamma Glutamyl Transferse (1.60 times normal, p < 0.001) as compared to 5’Nucleotidase (1.39 times normal, p < 0.01). Conclusion: Gamma Glutamyl Transferase and 5’Nucleotidase are useful for evaluation of not only obstructive biliary disease patients but also for the patients with biliary disease who are an-icteric, and out of these two, the former is a more valuable diagnostic indicator in such diseases

scholarly journals Studies on the subcellular localization of human neutrophil alkaline phosphatase

1979 ◽  
Vol 36 (1) ◽  
pp. 401-412
Author(s):  
G.J. Rustin ◽  
P.D. Wilson ◽  
T.J. Peters
Keyword(s):  
Alkaline Phosphatase ◽  
Endoplasmic Reticulum ◽  
Density Gradient ◽  
Human Neutrophil ◽  
Density Gradient Centrifugation ◽  
Gradient Centrifugation ◽  
Human Neutrophils ◽  
Gamma Glutamyl Transferase ◽  
Gamma Glutamyl ◽  
Glutamyl Transferase

The intracellular localization of alkaline phosphatase has been determined in human neutrophils with analytical subcellular fractionation by density gradient centrifugation and EM cytochemistry. Centrifugation on sucrose gradients containing 1 mM DETA and 5 units/ml of heparin showed that alkaline phosphatase was associated with a membranous component distinct from plasma membrane, mitochondria, specific granules and azurophil granules. There was no resolution from the endoplasmic reticulum. Density gradient centrifugation on a sucrose-imidazole-heparin gradient showed a clear resolution of the alkaline phosphatase-containing membranes from the Golgi and endoplasmic reticulum. Density gradient centrifugation of neutrophils that had been disrupted in the presenceof 0.12 mmol/l. digitonin clearly separated alkaline phosphatase-containing membranes from the endoplasmic reticulum. Part of the gamma-glutamyl transferase has a similar localization to that of alkaline phosphatase. EM cytochemistry of neutrophils, neutrophil homogenates and of the density gradient fractions identified alkaline phosphatase-containing granules as irregular-shaped, often tubular, structures. It is suggested that alkaline phosphatase and part of the gamma-glutamyl transferase activity are localized to a unique organelle in the human neutrophil.

scholarly journals Blood plasma chemistry in White Sea bearded seals across different age groups

2019 ◽  
Vol 19 (4) ◽  
pp. 159-165
Author(s):  
IA Erokhina ◽  
NN Kavtsevich
Keyword(s):  
Alkaline Phosphatase ◽  
Creatine Kinase ◽  
Uric Acid ◽  
Lactate Dehydrogenase ◽  
White Sea ◽  
Blood Chemistry ◽  
Total Lipids ◽  
Bearded Seal ◽  
Γ Globulins ◽  
Glutamyl Transferase

Blood chemistry values are reported for the bearded seal species (Erignathus barbatus barbatus Erxleben, 1777) from the White Sea. 27 blood plasma indices are used to describe the state of the metabolism of proteins, carbohydrates, lipids, minerals (total protein, albumin, α-, β-, γ-globulins, urea, creatinine, uric acid, glucose, lactic acid, total lipids, triglycerides, cholesterol, calcium, phosphorus, sodium, potassium, magnesium, iron, copper, chlorides, aspartate aminotransferase, alanine aminotransferase, γ-glutamyl transferase, creatine kinase, alkaline phosphatase, lactate dehydrogenase) in 3-, 5- and 10-year-old seals. The values of the studied parameters are similar to published data for bearded seal populations in other Arctic regions, as well as being in close agreement with indicators of other pinniped species of the same age. The plasma content of total protein, albumin, α-, β-, γ-globulins, urea, uric acid, total lipids, calcium, magnesium, sodium, and chlorides is invariable in animals of the studied ages. In common with other pinnipeds and land-based mammals, age-related changes in metabolic rates in the studied animal groups are most pronounced in the activity level of key metabolism enzymes. While aspartate aminotransferase, alanine aminotransferase and γ-glutamyl transferase activity is higher in adult seals than in immature animals, alkaline phosphatase, creatine kinase and lactate dehydrogenase activity is lower. Changes in biochemical parameters of bearded seal blood at the ages of 3, 5 and 10 years indicate a catabolic orientation in metabolism at all studied development stages. Although more research is needed to investigate the biological significance of a number of blood indices, the data presented in this study provide initial baseline blood chemistry parameters for use in assessing the condition of individual seals, as well as informing monitoring and management efforts for wild seal populations.

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