Horse brain acylphosphatase: purification and characterization.
Abstract: Two structurally different acylphosphatases found in horse brain were purified; they were not immunologically related. The molecular masses were almost identical and the kinetic parameters were rather similar. The data reported indicate that one of the purified brain acylphosphatases and an enzyme, previously isolated from horse muscle, are the same protein. The presence of this acylphosphatase form in the brain has not been reported before. The other acylphosphatase seemed to be the same as the enzyme which had been purified from calf brain and partially characterized by Diederich and Grisolia [(1969) J. Biol. Chem. 244, 2412-2417]. Furthermore, this enzyme seems to be identical to the acylphosphatase recently purified in our laboratory from human erythrocytes.
Publication Date: 1988-08-15 PubMed ID: 2841163DOI: 10.1016/0014-5793(88)80316-8Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The researchers successfully purified two types of acylphosphatases, structural enzymes, from a horse’s brain – one of them is reportedly identical to a previously discovered muscle enzyme, marking its first recording in the brain. The second enzyme seems to match an enzyme from calf brains and human erythrocytes.
Research Overview
- The study focuses on the purification and characterization of two structurally different acylphosphatases from a horse’s brain.
- These enzymes were found to be not immunologically related, which means they did not react to the same set of antigens (foreign substances that trigger an immune response).
- Despite this difference, they had nearly identical molecular masses and their kinetic parameters, indicating how the enzymes reacted to changes in substrate concentration, were quite similar.
Findings
- An interesting finding of this study was that one of these brain acylphosphatases turned out to be the same enzyme previously isolated from horse muscle tissue. This was a new discovery as this particular form of the enzyme wasn’t reported in the brain before.
- The other acylphosphatase appeared identical to an enzyme purified from calf brains, as characterized in a previous study by Diederich and Grisolia in 1969.
- This same enzyme seems to be identical to an acylphosphatase recently purified from human erythrocytes (red blood cells) in their own laboratory.
Conclusion
- Overall, the study has expanded the understanding of acylphosphatases in equine brains, also providing fresh insights into enzyme homology (similarity due to shared ancestry) across different species and tissues – horse muscle, calf brain, and human erythrocytes.
- In future, these findings might prove beneficial in studying the roles of these enzymes in cellular processes, their possible impact on medical science, and discerning their evolutionary pathways.
Cite This Article
APA
Stefani M, Berti A, Camici G, Manao G, Degl'Innocenti D, Prakash G, Marzocchini R, Ramponi G.
(1988).
Horse brain acylphosphatase: purification and characterization.
FEBS Lett, 236(1), 209-216.
https://doi.org/10.1016/0014-5793(88)80316-8 Publication
Researcher Affiliations
- Department of Biochemistry, University of Florence, Italy.
MeSH Terms
- Acid Anhydride Hydrolases
- Amino Acids / analysis
- Animals
- Brain / enzymology
- Chromatography, Affinity
- Chromatography, Gel
- Chromatography, High Pressure Liquid
- Erythrocytes / enzymology
- Horses
- Immunoassay
- Immunodiffusion
- Muscles / enzymology
- Phosphoric Monoester Hydrolases / isolation & purification
- Phosphoric Monoester Hydrolases / metabolism
- Acylphosphatase
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