The apo-enzyme content of aminotransferases in healthy and diseased domestic animals.
Abstract: We investigated the apo-enzyme content of alanine aminotransferase (ALT) and aspartate aminotransferase (AST) in clinically normal and ill canine, feline, equine and bovine patients. Aminotransferase activity was measured with and without the addition of exogenous pyridoxal-5'-phosphate (P5P). The amount of apo-enzyme was expressed as the percentage change in aminotransferase activity with the inclusion of P5P. The results of aminotransferase assays without P5P (holo-enzyme activity) were highly correlated to the results obtained with P5P (total enzyme activity) in all four species (Spearman rank correlations > 0.980). The median apo-aminotransferase percentage in clinically normal patients was: 11% ALT and 0% AST in 115 dogs, 7% ALT and -5% AST in 50 cats, 6% AST in 46 horses and 9% AST in 50 cattle. The amount of apo-enzyme did not increase as holo-enzyme activity increased in any of the species. The apo-aminotransferase content was not significantly different in canine, feline and equine patients with diseases affecting the liver, kidney or musculature compared to clinically normal animals. The apo-enzyme content did not differ significantly between specific liver diseases in canine and feline patients.
Publication Date: 2002-06-21 PubMed ID: 12075541DOI: 10.1111/j.1939-165x.1998.tb01022.xGoogle Scholar: Lookup The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Journal Article
Summary
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This research investigates the content of two apo-enzymes, alanine aminotransferase (ALT) and aspartate aminotransferase (AST), in various species of healthy and sick domestic animals. The study concludes that the amounts of these apo-enzymes do not notably increase with increasing holo-enzyme activity and are not significantly different in animals with certain diseases compared to healthy ones.
Explanation of Methodology
- The researchers evaluated the content of ALT and AST in four species of domestic animals, including dogs, cats, horses, and cattle. Half of the subjects were healthy, while the others were suffering from various illnesses
- The method involved testing for enzymatic activity with and without the addition of an external source of pyridoxal-5′-phosphate (P5P), a coenzyme that is necessary for the functioning of ALT and AST
- The concentration of the apo-enzyme (the enzyme without its necessary coenzyme, P5P) was then quantified as the percentage change in enzymatic activity when P5P was added to the assay
Results and Findings
- The findings showed a strong correlation between the enzymatic activities measured with and without the addition of P5P in all the species studied. This means that these enzymes largely function the same way, regardless of the presence or absence of the coenzyme
- Apo-enzyme percentages in regular, healthy subjects varied across species, but the amount did not increase as the holo-enzyme activity (the activity of the enzyme with its coenzyme) increased
- The study also found that the amount of apo-enzyme in diseased animals (canine, feline, and equine patients with liver, kidney, or muscle diseases) was not significantly different compared to the healthy animals
Implications of the Study
- The study implies that these two enzymes function in a largely consistent fashion across various species and disease states
- This lack of variation in enzyme content could suggest that variations in the health or disease state of the animals do not significantly affect the functioning of these enzymes
- However, more research may be needed to investigate whether other factors could potentially influence the functioning of these enzymes
Cite This Article
APA
Stokol T, Erb H.
(2002).
The apo-enzyme content of aminotransferases in healthy and diseased domestic animals.
Vet Clin Pathol, 27(3), 71-78.
https://doi.org/10.1111/j.1939-165x.1998.tb01022.x Publication
Researcher Affiliations
- Department of Pathology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.
Citations
This article has been cited 2 times.- Chen G, Shui S, Chai M, Wang D, Su Y, Wu H, Sui X, Yin Y. Effects of Paper Mulberry (Broussonetia papyrifera) Leaf Extract on Growth Performance and Fecal Microflora of Weaned Piglets. Biomed Res Int 2020;2020:6508494.
- Berdyshev EV, Goya J, Gorshkova I, Prestwich GD, Byun HS, Bittman R, Natarajan V. Characterization of sphingosine-1-phosphate lyase activity by electrospray ionization-liquid chromatography/tandem mass spectrometry quantitation of (2E)-hexadecenal. Anal Biochem 2011 Jan 1;408(1):12-8.
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