Abstract
The proposed amino acid sequence of porcine LH- and FSH-releasing hormone (LH-RH/FSH-RH) was reinvestigated by Edman-dansyl degradation after the cleavage of N-terminal pyroglutamyl residue by pyrrolidonecarboxylyl (PCA) peptidase. A C-terminal fragment from chymotrypic digest of LH-RH/FSH-RH was found to be identical to synthetic Gly-Leu-Arg-Pro-Gly-NH2. The results indicate that the structure initially proposed is correct. The amino acid sequence of porcine LH-RH/FSH-RH is thus (pyro)Glu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH2.
Original language | English (US) |
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Pages (from-to) | 459-463 |
Number of pages | 5 |
Journal | Biochemical and biophysical research communications |
Volume | 44 |
Issue number | 2 |
DOIs | |
State | Published - Jul 16 1971 |
Externally published | Yes |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology