Neurohypophysial granule Ca2+-dependent endopeptidases have been allowed to act on synthetic polypeptides derived from the N-terminal sequence of bovine provasopressin-neurophysin, namely vasopressinyl-glycyl-lysyl-arginyl-alanylamide and vasopressinyl-glycyl-lysyl-arginyl-alanyl-methionyl-serinamide. Membrane-bound enzymes have been used at pH5.5 for 16 hr at 37 °C. Products have been identified by high-pressure liquid chromatography (HPLC) and by mass spectrometry performed on substances isolated by HPLC. With both substrates, vasopressinyl-Gly-Lys-Arg(OH) has been identified as a product confirming the Lys-Arg specificity previously observed on small peptide fluorogenic substrates. Cleavage yields, however, appear low suggesting that some factors are missing, for example a targeting action of the precursor neurophysin domain to the granule membrane.
Action of neurohypophysial granule Lys-Arg endopeptidase on synthetic polypeptides comprising the processing sequence of provasopressin-neurophysin
- Views Icon Views
- PDF LinkPDF
- Share Icon Share
- Cite Icon Cite
Gilles Michel, Yves Rouille, Jacqueline Chauvet, Roger Acher; Action of neurohypophysial granule Lys-Arg endopeptidase on synthetic polypeptides comprising the processing sequence of provasopressin-neurophysin. Biosci Rep 1 August 1994; 14 (4): 171–178. doi: https://doi.org/10.1007/BF01200246
Download citation file: