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Processing of chromogranin A within chromaffin granules starts at C‐ and N‐terminal cleavage sites
Author(s) -
Wohlfarter Thomas,
Fischer-Colbrie Reiner,
Hogue-Angeletti Ruth,
Eiden Lee E.,
Winkler Hans
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80704-x
Subject(s) - chromogranin a , antiserum , cleavage (geology) , immunostaining , endogeny , chemistry , proteolysis , proteases , chromaffin cell , peptide , oligopeptide , biochemistry , microbiology and biotechnology , biology , adrenal medulla , endocrinology , enzyme , immunohistochemistry , antigen , immunology , catecholamine , paleontology , fracture (geology)
Specific antisera were raised against synthetic peptide fragments of bovine chromogranin A. The soluble proteins of bovine chromaffin granules were subjected to two‐dimensional immunoblotting with these antisera. The endogenous breakdown products of chromogranin A gave distinct patterns of immunostaining which enabled us to correlate these peptides with defined regions of the chromogranin A molecule. The results establish that within chromaffin granules degradation of chromogranin A by the endogenous proteases can start either at the C‐ or the N‐terminal site.