Occurrence and nature of equine and bovine myoglobin dimers.
Abstract: In commercial samples of equine myoglobin and samples of equine and bovine myoglobin prepared in the laboratory, a small amount of the protein was present as an aggregate. The presence of the myoglobin aggregate could be demonstrated by gel filtration on Sephadex G-100 Superfine, which also provided a means of isolating it. Gel filtration on Sephadex G-100 showed the molecular weights of the equine and bovine moyglobin aggregates to be about 35000 and 34000 respectively, thus supporting the hypothesis that they are dimers. This was confirmed for the equine myoglobin by ultracentrifugation measurements.
The exact nature of the dimer cannot be specified. The conditions required for its formation in vitro and the fact that no traces of dimer could be detected in fresh muscle preclude the possibility of its natural occurrence. The spectral properties of the equine myoglobin dimer and its sedimentation and diffusion behaviour in the ultracentrifuge indicate, however, that the configuration of native monomeric myoglobin is essentially preserved in the dimer.
Like their respective monomers, the dimers of equine and bovine myoglobin were shown by isoelectric fractionation to be microheterogeneous.
Publication Date: 1969-08-01 PubMed ID: 5345978DOI: 10.1111/j.1432-1033.1969.tb00665.xGoogle Scholar: Lookup
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- Journal Article
Summary
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The research article presents a study that investigates the occurrence and nature of protein aggregates, referred to as dimers, in equine and bovine myoglobin. The research data supports the hypothesis that these aggregates are dimers, and while their exact nature is unclear, the research finds no evidence of their natural occurrence in fresh muscle.
Identification and Isolation of Protein Aggregates
- The research found that small amounts of protein were present as aggregates, specifically in commercial samples of equine myoglobin and lab-prepared samples of equine and bovine myoglobin.
- The presence of these myoglobin aggregates was demonstrated using gel filtration on Sephadex G-100 Superfine, which also provided a method for isolating these aggregates.
Support for the Dimer Hypothesis
- Gel filtration data showed the molecular weights of the equine and bovine myoglobin aggregates to be approximately 35000 and 34000 respectively, supporting the hypothesis that these aggregates are dimers – protein complexes made up of two, typically identical, molecules.
- This was further confirmed for equine myoglobin through ultracentrifugation measurements, an experimental procedure used to determine properties such as size and density of particles in a solution.
Nature of the Dimer
- The nature of the dimer is unclear due to the specific conditions needed for its in vitro formation, and the lack of traces in fresh muscle, ruling out the possibility of its natural occurrence.
- The spectral properties of the equine myoglobin dimer, as well as its behavior in the ultracentrifuge, however, suggest that the configuration of the original single myoglobin molecule (monomer) is essentially preserved in the dimer.
Dimer Microheterogeneity
- The research also reveals that like their respective monomers, the dimers of equine and bovine myoglobin were found to be microheterogeneous through isoelectric fractionation, a technique used to separate proteins based on their isoelectric point (the pH at which the protein carries no net electrical charge).
Cite This Article
APA
Van den Oord AH, Wesdorp JJ, Van Dam AF, Verheij JA.
(1969).
Occurrence and nature of equine and bovine myoglobin dimers.
Eur J Biochem, 10(1), 140-145.
https://doi.org/10.1111/j.1432-1033.1969.tb00665.x Publication
Researcher Affiliations
MeSH Terms
- Animals
- Cattle
- Chemical Phenomena
- Chemistry
- Chromatography, Gel
- Dextrans
- Dialysis
- Drug Stability
- Electrophoresis
- Ferricyanides
- Freeze Drying
- Hemoglobins
- Horses
- Hydrogen-Ion Concentration
- Methods
- Molecular Weight
- Muscles / analysis
- Myocardium
- Myoglobin / isolation & purification
- Ultracentrifugation
Citations
This article has been cited 7 times.- Scrima R, Agriesti F, Pacelli C, Piccoli C, Pucci P, Amoresano A, Cela O, Nappi L, Tataranni T, Mori G, Formisano P, Capitanio N. Myoglobin expression by alternative transcript in different mesenchymal stem cells compartments. Stem Cell Res Ther 2022 May 21;13(1):209.
- Piccinini A, Lourenço EC, Ascenso OS, Ventura MR, Amenitsch H, Moretti P, Mariani P, Ortore MG, Spinozzi F. SAXS Reveals the Stabilization Effects of Modified Sugars on Model Proteins. Life (Basel) 2022 Jan 15;12(1).
- Schneider CM, Cölfen H. Analytical band centrifugation revisited. Eur Biophys J 2018 Oct;47(7):799-807.
- Trana EN, Nocek JM, Woude JV, Span I, Smith SM, Rosenzweig AC, Hoffman BM. Charge-Disproportionation Symmetry Breaking Creates a Heterodimeric Myoglobin Complex with Enhanced Affinity and Rapid Intracomplex Electron Transfer. J Am Chem Soc 2016 Sep 28;138(38):12615-28.
- Fowler CB, Evers DL, O'Leary TJ, Mason JT. Antigen retrieval causes protein unfolding: evidence for a linear epitope model of recovered immunoreactivity. J Histochem Cytochem 2011 Apr;59(4):366-81.
- Gray JC, Kekwick RG. Mevalonate kinase in green leaves and etiolated cotyledons of the french bean Phaseolus vulgaris. Biochem J 1973 Jun;133(2):335-47.
- Romero-Herrera AE, Lehmann H, Tomlinson BE, Walton JN. Myoglobin in primary muscular disease. I. Duchenne muscular dystrophy. II. Muscular dystrophy of distal type. J Med Genet 1973 Dec;10(4):309-22.
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