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Immunological Characterization of Secretory Proteins of Chromaffin Granules: Chromogranins A, Chromogranins B, and Enkephalin‐Containing Peptides
Author(s) -
FischerColbrie R.,
Frischenschlager I.
Publication year - 1985
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1985.tb07179.x
Subject(s) - antiserum , adrenal medulla , chromogranin a , secretory protein , biochemistry , chemistry , chromaffin cell , cell fractionation , biology , microbiology and biotechnology , secretion , enzyme , antibody , catecholamine , immunology , endocrinology , immunohistochemistry
The soluble proteins of bovine chromaffin granules can be resolved into about 40 proteins by twodimensional electrophoresis. Use of several antisera enabled us to characterize most of these proteins with the immune replica technique. An antiserum against dopamine β‐hydroxylase reacted with one protein of M r 75,000. Met‐enkephalin antisera labeled eight proteins of M r 23,000–14,000. A new method was developed to obtain highly purified chromogranin A for immunization. The antiserum reacted with chromogranin A and several smaller proteins of similar pI. This specific antiserum did not react with a second family of hitherto undescribed proteins, which we propose to call chromogranins B. An antiserum against these proteins was raised. It labeled several proteins ranging in M r from 100,000 to 24,000 and focusing at pH 5.2. Subcellular fractionation established that chromogranins B are specifically localized in chromaffin granules of several species. They are secreted from the adrenal medulla during cholinergic stimulation. We conclude that apart from dopamine β‐hydroxylase chromaffin granules contain three families of immunologically unrelated proteins.