| Autor: |
Govorun MS, Osipova TA, Khil'ko SN, Martynov AV, Bulatov AA |
| Jazyk: |
ruština |
| Zdroj: |
Nauchnye doklady vysshei shkoly. Biologicheskie nauki [Nauchnye Doki Vyss Shkoly Biol Nauki] 1992 (7), pp. 74-80. |
| Abstrakt: |
Stability of heterodimers of human glycoprotein hormones with gonadotropic and thyrotropic activities in sodium dodecylsulfate (SDS) under non-reducing conditions at low temperature permits to resolve the native molecules of these hormones in SDS-PAG and to distinguish from their dissociated subunits by electrophoretical mobility. The analysis of dimers and alpha-, beta-subunits in one polyacrylamide gel allows to detect certain human glycoprotein hormones and to study some of their physico-chemical properties. Using two polyclonal antisera against human LH and FSH by the Western blot immunoassay it was shown that heterodimers as well as alpha and beta subunits after SDS-PAGE retain antigenic activity of native hormones. The method gave possibility to characterize the specificity of the given sera to different glycoprotein hormones. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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