Abstract
Two forms of gonadotropin-releasing hormone (GnRH) have been purified from brain extracts of the African catfish, Clarias gariepinus, using reverse- phase high performance liquid chromatography (HPLC) and radioimmunoassay (RIA). The amino acid sequences of both forms of African catfish GnRH were determined using Edman degradation after digestion with pyroglutamyl aminopeptidase. In addition, both GnRHs were studied by mass spectrometry. The primary structure of African catfish GnRH I is identical to Thai catfish GnRH I, pGlu-His-Trp-Ser-His-Gly-Leu-Asn-Pro-Gly-NH2, and the primary structure of African catfish GnRH II is identical to the widely distributed and highly conserved chicken GnRH II, pGlu-His-Trp-Ser-His-Gly-Trp-Tyr-Pro- Gly-NH2.
Original language | English |
---|---|
Pages (from-to) | 127-134 |
Number of pages | 8 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 187 |
Issue number | 1 |
Publication status | Published - 6 Sept 1992 |
Keywords
- gonadorelin
- amino acid sequence
- animal cell
- article
- binding affinity
- brain tissue
- catfish
- cellular distribution
- degradation
- gonadotropin release
- hormone release
- mass spectrometry
- nonhuman
- priority journal
- radioimmunoassay
- receptor binding
- reversed phase high performance liquid chromatography