Conformational analysis and proteolytic processing of synthetic pre-pro-GnRH/GAP protein
- 1 April 1993
- journal article
- Published by Springer Nature in Protein Journal
- Vol. 12 (2) , 133-141
- https://doi.org/10.1007/bf01026034
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- GAP-releasing enzyme is a member of the pro-hormone convertase family of precursor protein processing enzymesLife Sciences, 1993
- Characterization of homogeneous atrial granule serine proteinase, a candidate processing enzyme of pro-atrial natriuretic factorLife Sciences, 1992
- Total solid-phase synthesis and prolactin-inhibiting activity of the gonadotropin-releasing hormone precursor protein and the gonadotropin-releasing hormone associated peptideBiochemistry, 1992
- Design and synthesis of a helix heparin-binding peptideBiochemistry, 1992
- Kinetic analysis of the acid and the alkaline unfolded states of staphylococcal nucleaseJournal of Molecular Biology, 1991
- Consensus sequence for processing of peptide precursors at monobasic sitesFEBS Letters, 1991
- Solution phase conformation studies of the prekallikrein binding domain of high molecular weight kininogenProtein Journal, 1990
- Partial purification and functional properties of an endoprotease from bovine neurosecretory granules cleaving prooxytocin/neurophysin peptides at the basic amino acid doubletBiochemistry, 1987
- Stimulation of Gonadotropin Release by a Non-GnRH Peptide Sequence of the GnRH PrecursorScience, 1986
- Biosynthesis of LHRH: Inferences from immunocytochemical studiesPeptides, 1983