Purification and Characteristics of the Candidate Prohormone Processing Proteases PC2 and PC1/3 from Bovine Adrenal Medulla Chromaffin Granules
Open Access
- 1 April 1995
- journal article
- Published by Elsevier
- Vol. 270 (14) , 8201-8208
- https://doi.org/10.1074/jbc.270.14.8201
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- A Novel Member, PC7, of the Mammalian Kexin-like Protease Family - Homology to PACE4A, Its Brain-Specific Expression and Identification of IsoformsBiochemical and Biophysical Research Communications, 1994
- Unique cleavage specificity of ‘prohormone thiol protease’ related to proenkephalin processingFEBS Letters, 1994
- Furin has the proalbumin substrate specificity and serpin inhibitory properties of an in situ hepatic convertaseFEBS Letters, 1994
- Processing of prodynorphin by the prohormone convertase PC1 results in high molecular weight intermediate formsFEBS Letters, 1994
- Prohormone Thiol Protease and Enkephalin Precursor Processing: Cleavage at Dibasic and Monobasic SitesJournal of Neurochemistry, 1992
- Immunological characterization of the endoproteases PC1 and PC2 in adrenal chromaffin granules and in the pituitary glandFEBS Letters, 1992
- Characterization of PC2, a mammalian Kex2 homologue, following expression of the cDNA in microinjected Xenopus oocytesFEBS Letters, 1991
- Cleavage of recombinant enkephalin precursor by endoproteolytic activity in bovine chromaffin granulesBiochemical and Biophysical Research Communications, 1990
- Yeast KEX2 gene encodes an endopeptidase homologous to subtilisin-like serine proteasesBiochemical and Biophysical Research Communications, 1988
- The Determination of Enzyme Dissociation ConstantsJournal of the American Chemical Society, 1934