Discrimination of mammalian growth hormones by peptide-mass mapping.
Abstract: Recognition by the legal authorities that growth hormones (GHs) may be abused to improve sporting performance and/or physique has led to the implementation of controls that make it an offence to produce, supply, possess or import and export GHs, with intent to supply, without the authority to do so. A method is described for the discriminatory analysis of human, equine, porcine and bovine GHs for forensic purposes. Peptide-mass mapping by matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry following tryptic digestion gave sequence coverages of 97.4%, 93.7%, 94.2% and 90.6% for human, equine, porcine and bovine GHs respectively. The tryptic-mass maps generated were sufficient to discriminate between the four hormones analysed and thus provide unambiguous identification of each individual GH. Identification of the N-terminal peptides of recombinant equine and porcine GHs, which possess additional methionine residues, within the tryptic-mass maps may provide the basis of a test to indicate exogeneous administration rather than endogenous secretion of GH in performance dogs and horses.
Publication Date: 1998-07-31 PubMed ID: 9684382DOI: 10.1002/(SICI)1097-0231(19980731)12:14<975::AID-RCM263>3.0.CO;2-HGoogle Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This research paper outlines a method to distinguish between human, equine, porcine and bovine growth hormones, which could potentially be misused to improve sporting performance or physical appearance. The method makes use of peptide-mass mapping by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry following tryptic digestion.
Objective of the Research
- The research primarily aims to establish a reliable method to separate human, equine, porcine, and bovine growth hormones (GHs). The motivation behind this is to prevent the illegal use of GHs to enhance sporting performance or improve physical attributes, as GHs can be abused for such purposes.
Methodology
- Researchers have used peptide-mass mapping with the help of matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry post tryptic digestion.
- Through this process, the team was able to attain sequence coverage of 97.4%, 93.7%, 94.2%, and 90.6% for human, equine, porcine, and bovine GHs respectively. This means that the majority of each type of GH was mapped in this process.
Findings
- The mass maps generated using this technique were adequate to distinguish between the four hormones studied.
- The results led to the unequivocal identification of each GH, making it easier to identify misuse.
- Moreover, identifying the N-terminal peptides of recombinant equine and porcine GHs, which carry additional methionine residues within the tryptic-mass maps, could indicate whether GH has been externally administered rather than naturally secreted in performance dogs and horses.
Implications
- The development of a reliable GH discrimination method contributes towards the prevention of illegal GH use to enhance sports performance or physical appearance.
- By being able to tell apart different types of GH and identifying exogeneous administration, regulatory bodies and sports authorities may have a new tool to ensure fairness and safety in both human and animal sports competitions.
Cite This Article
APA
Laidler P, Cowan DA, Houghton E, Kicman AT, Marshall DE.
(1998).
Discrimination of mammalian growth hormones by peptide-mass mapping.
Rapid Commun Mass Spectrom, 12(14), 975-981.
https://doi.org/10.1002/(SICI)1097-0231(19980731)12:14<975::AID-RCM263>3.0.CO;2-H Publication
Researcher Affiliations
- Drug Control Centre, King's College London, UK.
MeSH Terms
- Amino Acid Sequence
- Animals
- Cattle
- Growth Hormone / analysis
- Horses
- Humans
- Hydrolysis
- Molecular Sequence Data
- Peptide Mapping
- Species Specificity
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- Swine
- Trypsin
Citations
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