Studies on a number of erythrocytic enzymes and intermediate products of equine erythrocyte metabolism.
Abstract: The activities and concentrations of a number of erythrocytic enzymes and intermediate products of erythrocyte metabolism were determined in twenty-one normal standard-bred horses which were studied clinically and biochemically. These studies showed that equine anaerobic glycolysis is characterized by a biochemical pattern similar to that observed in human PK deficiency. The greater sensitivity of equine haemoglobin to oxidants is attributable either to low stability of GSH, which may be due either to the low activity of GR or that of 6PGD as observed in the studies. In addition, the saturation of GOT and GR with cofactor and apoenzyme respectively were determined.
Publication Date: 1977-10-15 PubMed ID: 918926
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- Comparative Study
- Journal Article
Summary
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This research article investigated the activities and concentrations of various enzymes and intermediate products related to red blood cell metabolism in normal standard-bred horses, finding similarities to human PK deficiency and exploring the reasons for equine haemoglobin’s high sensitivity to oxidants.
Research Context and Methodology
- This research was carried out to understand the metabolic activities that occur within the red blood cells (erythrocytes) of normal standard-bred horses.
- The study involved the analysis of several erythrocytic enzymes and intermediate products of erythrocyte metabolism.
- These enzymes and products were examined in twenty-one normal standard-bred horses, which were scrutinized both clinically and biochemically to ensure their normal status.
Research Findings
- The research revealed that the process of anaerobic glycolysis, a metabolic pathway that enables cell survival during hypoxia, has a biochemical pattern in horses comparable to that seen in human pyruvate kinase (PK) deficiency. Pyruvate kinase is an enzyme crucial for glycolysis, and its deficiency leads to a decrease in ATP production and the lifespan of red blood cells.
- Additionally, the study discovered that the high sensitivity of equine haemoglobin (the protein responsible for transporting oxygen in the bloodstream) to oxidants could be attributed to the reduced stability of glutathione (GSH), an antioxidant that protects cells from oxidative damage.
- The instability of GSH was linked to the possibly low activity of glutathione reductase (GR) or 6-phosphogluconate dehydrogenase (6PGD), both of which are enzymes involved in maintaining the health and integrity of red blood cells.
- In addition to these findings, the research also detailed the saturation levels of glutamic oxaloacetic transaminase (GOT) and glutathione reductase (GR) within their cofactor and apoenzyme respectively. This knowledge is crucial for understanding the functionality and regulation of these enzymes.
Implications of the Research
- This research contributes valuable insights into the red blood cell metabolic processes of normal standard-bred horses. These findings could be beneficial for developing treatments for horses with metabolic issues or anemia.
- The similarities between the horses’ erythrocyte metabolism and human PK deficiency could potentially stimulate development of novel therapeutic approaches for managing this condition in both species.
- Knowing about the sensitivity of equine haemoglobin to oxidants could potentially guide investigations into the resistance parameters of other animal species, which would hold significant value for comparative veterinary and medical study.
Cite This Article
APA
Franken P, Schotman JH.
(1977).
Studies on a number of erythrocytic enzymes and intermediate products of equine erythrocyte metabolism.
Tijdschr Diergeneeskd, 102(20), 1197-1203.
Publication
Researcher Affiliations
MeSH Terms
- Animals
- Erythrocytes / enzymology
- Glycolysis
- Horses / blood
- Humans
Citations
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