| Literature DB >> 3258015 |
S Rieker1, R Fischer-Colbrie, L Eiden, H Winkler.
Abstract
The presence of chromogranin-related peptides in a wide range of species was investigated by one and two-dimensional electrophoresis followed by immunoblotting. Antisera against bovine chromogranins A and B and the peptide WE-14 (chromogranin A316-329) were used. Chromogranins were identified by their heat stability, by their electrophoretic behavior, and by immunological cross-reaction with antisera. In all species investigated ranging from mammals to birds, amphibians, fish, and arthropods, chromogranin A- and B-like proteins could be demonstrated. For all species, there was an immunological cross-reaction with antisera against bovine chromogranins. The molecular sizes and isoelectric points of the chromogranins were similar in all species. The antiserum against WE-14 cross-reacted with pig, rat, and chicken chromogranins. It is concluded that the chromogranins A and B have a widespread phylogenetic distribution with a significant conservation of molecular size, isoelectric points, and immunological epitopes. This is consistent with the concept that these peptides have a specific function.Entities:
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Year: 1988 PMID: 3258015 DOI: 10.1111/j.1471-4159.1988.tb10574.x
Source DB: PubMed Journal: J Neurochem ISSN: 0022-3042 Impact factor: 5.372