Age-Dependent Variations of Lactate Dehydrogenase and Creatine Kinase Activities in Water Buffalo Calf Serum

Avallone, Luigi; Lombardi, Pietro; Florio, Salvatore; D’Angelo, Antonio; Bogin, E.

doi:10.1515/cclm.1996.34.12.961

Cited by 7 publications

(7 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Avallone et al found that lactate dehydrogenase is heat stable and retains most of its activity up to 70 °C; it, then, loses its activity upon further heating. This agrees with the presence of the spots indicating lactate dehydrogenase, where we observed a band at 63 °C, which was absent at 98 °C [38]. The enzyme levels in buffalo milk are used as markers for pasteurization because of their sensitivity to heat inactivation [39].…”

Section: Resultssupporting

confidence: 84%

Proteomic Profiling Comparing the Effects of Different Heat Treatments on Camel (Camelus dromedarius) Milk Whey Proteins

Benabdelkamel

Alanazi

Alzahrani

et al. 2017

IJMS

View full text Add to dashboard Cite

Camel milk is consumed in the Middle East because of its high nutritional value. Traditional heating methods and the duration of heating affect the protein content and nutritional quality of the milk. We examined the denaturation of whey proteins in camel milk by assessing the effects of temperature on the whey protein profile at room temperature (RT), moderate heating at 63 °C, and at 98 °C, for 1 h. The qualitative and quantitative variations in the whey proteins before and after heat treatments were determined using quantitative 2D-difference in gel electrophoresis (DIGE)-mass spectrometry. Qualitative gel image analysis revealed a similar spot distribution between samples at RT and those heated at 63 °C, while the spot distribution between RT and samples heated at 98 °C differed. One hundred sixteen protein spots were determined to be significantly different (p < 0.05 and a fold change of ≥1.2) between the non-heated and heated milk samples. Eighty protein spots were decreased in common in both the heat-treated samples and an additional 25 spots were further decreased in the 98 °C sample. The proteins with decreased abundance included serum albumin, lactadherin, fibrinogen β and γ chain, lactotransferrin, active receptor type-2A, arginase-1, glutathione peroxidase-1 and, thiopurine S, etc. Eight protein spots were increased in common to both the samples when compared to RT and included α-lactalbumin, a glycosylation-dependent cell adhesion molecule. Whey proteins present in camel milk were less affected by heating at 63 °C than at 98 °C. This experimental study showed that denaturation increased significantly as the temperature increased from 63 to 98 °C.

show abstract

Section: Resultssupporting

confidence: 84%

Proteomic Profiling Comparing the Effects of Different Heat Treatments on Camel (Camelus dromedarius) Milk Whey Proteins

Benabdelkamel

Alanazi

Alzahrani

et al. 2017

IJMS

View full text Add to dashboard Cite

show abstract

“…Avallone et al [76] investigated the variations of LDH activities in young water buffalo calves. Differences in total activities as well as their relative distribution were seen at ages ranging from 1 to 10 weeks.…”

Section: The Effect Of Age Stress Exercise Breed Sex and Season mentioning

confidence: 99%

Clinical and Diagnostic Significance of Lactate Dehydrogenase and Its Isoenzymes in Animals

Klein

Nagy

Tóthová

et al. 2020

Veterinary Medicine International

106

View full text Add to dashboard Cite

Lactate dehydrogenase (LDH) is widely distributed enzyme in cells of various living systems where it is involved in carbohydrate metabolism catalyzing interconversion of lactate and pyruvate with NAD+/NADH coenzyme system. Cells of tissues are direct source of lactate dehydrogenase isoenzymes that are naturally distributed in blood plasma/serum of animals and humans producing characteristic profile. This profile depends on intracellular isoenzyme concentration in all tissues that contribute to the common pool of lactate dehydrogenases in plasma/serum as a consequence of natural cell degradation. LDH is widely distributed in the body, high activities are found in the heart, liver, skeletal muscle, kidney, and erytrocytes, whereas lesser amounts are found in the lung, smooth muscle, and brain. Because of its widespread activities in numerous body tissues, LDH is elevated in a variety of disorders. There are many conditions that contribute to increased activity of LDH. An elevated total LDH value is a rather nonspecific finding. Therefore, LDH assays assume a more clinical significance when separated into isoenzyme fractions. The activity of LDH and its serum and tissue patterns and composition show great variations between the species. These differences do not allow using catalytic activities of LDH isoenzymes from one species to another. Instead, the pattern of serum LDH isoenzymes should be interpreted in respect to its species origin that is important in particular in veterinary medicine. Determination of total LDH activity and its isoenzyme pattern in serum of mammals had become one of the biochemical indicators in the assessment of organ disorders. When the content of cells is released from tissue to plasma, as on cell injury, the LDH isoenzyme pattern of the serum changes in favour of the profile of the affected organ (tissue) that can be used in the diagnostic practice.

show abstract

“…Avallone et al 22 recorded insignificant change in the total LDH, a reduction in LDH 1 and LDH 5 , an increase in LDH 2 and LDH 3 and no change in LDH 4 relative activities in water buffalo calf serum accompanying aging. In the same context, Prathima and Devi 23 have reported that blood LDH activity decreased with age and that swim training in rats induced elevations in the enzyme activity.…”

Section: Aging Antioxidants and Isoenzymes 141mentioning

confidence: 96%

Protective effects of antioxidants on age‐related changes in the electrophoretic patterns of cardiac LDH, hepatic ALP and serum proteins in male golden hamster

El-Zayat

Amer

2003

Cell Biochemistry & Function

View full text Add to dashboard Cite

Basal and antioxidant-induced changes in the isoenzyme and isoform patterns of cardiac lactate dehydrogenase (EC 1.1.1.27) and hepatic alkaline phosphatase (EC 3.1.3.1), respectively, as well as the electrophoretic patterns of serum proteins in different age groups of male golden hamster were compared. This is to test whether age-induced changes could be corrected by long-term administration of antioxidants. Data indicated that aging causes no remarkable change in the total activity of either cardiac LDH or hepatic ALP, however a significant increase in the fractional activity of some cardiac LDH isoenzymes and a significant reduction in the fractional activity of some hepatic ALP isoforms were induced by aging. On the other hand, long-term administration of antioxidants appeared to manifest a clear counteracting effect on the age-related changes in old age. This effect was indicated in the fractional activity of cardiac LDH isoenzymes and of hepatic ALP isoforms. The present study has also shown a wide-range variation in serum protein patterns due to aging and/or antioxidant administration, which indirectly reflect a parallel variation in the process of gene expression and/or proteolytic activity.

show abstract

Age-Dependent Variations of Lactate Dehydrogenase and Creatine Kinase Activities in Water Buffalo Calf Serum

Cited by 7 publications

References 5 publications

Proteomic Profiling Comparing the Effects of Different Heat Treatments on Camel (Camelus dromedarius) Milk Whey Proteins

Proteomic Profiling Comparing the Effects of Different Heat Treatments on Camel (Camelus dromedarius) Milk Whey Proteins

Clinical and Diagnostic Significance of Lactate Dehydrogenase and Its Isoenzymes in Animals

Protective effects of antioxidants on age‐related changes in the electrophoretic patterns of cardiac LDH, hepatic ALP and serum proteins in male golden hamster

Contact Info

Product

Resources

About