Abstract
Human growth hormone (GH) has several central metabolic functions including bone growth in childhood and its anabolic and lipolytic effects in particular are assumed reasons for the abuse of GH by athletes. Human endogenous GH consists of a main 22 kDa variant and several isoforms. In contrast, recombinant GH consists of only one variant being identical to the main endogenous isoform. The method presented here separates different isoforms by 2D-PAGE after isolation of growth hormone from plasma using an immunoaffinity purification system. While samples containing endogenous GH yield up to four isoforms, samples with recombinant GH are supposed to contain the main 22 kDa spot only. External stimuli like exercise trigger the release of growth hormone from the pituitary. It was shown that the release is detected by the presented method as an increase in all isoforms. This approach detects isoforms of GH from plasma and discriminates endogenous GH from its recombinant analog which makes it a useful approach for doping control purposes. Verf.-Referat
| Original language | German |
|---|---|
| Title of host publication | Recent advances in doping analysis (16) : Proceedings of the Manfred Donike Workshop ; 26th Cologne Workshop on Dope Analysis, 24th to 29th February 2008 |
| Editors | Wilhelm Schänzer, Hans Geyer, A. Gotzmann, Ute Mareck |
| Number of pages | 11 |
| Publisher | Sportverlag Strauß |
| Publication date | 2008 |
| Pages | 233-243 |
| Publication status | Published - 2008 |
| Event | Cologne Workshop on Dope Analysis - Köln, Germany Duration: 24.02.2008 → 29.02.2008 Conference number: 26 |