ISSN:
1573-4935
Keywords:
granule Lys-Arg endopeptidase
;
neurohypophysial granules
;
vasopressinyl-peptide processing
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01200246
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