| Literature DB >> 10814538 |
D Rodríguez-Agudo1, M T Olmo, F Sánchez-Jiménez, M A Medina.
Abstract
We have followed the in vitro degradation of rat histidine decarboxylase in a reconstituted system, containing only rat histidine decarboxylase (obtained by in vitro transcription and translation), calcium ions in the millimolar range of concentrations, and m-calpain. Under the experimental conditions used, m-calpain quickly and efficiently degraded rat histidine decarboxylase, giving rise to a major proteolytic band of 29 kDa. In a conventional in vitro degradation system containing rabbit reticulocytes supplemented with calcium ions, there was also an intense proteolysis of rat histidine decarboxylase, strongly inhibited in the presence of calpeptin, a highly specific calpain inhibitor. Copyright 2000 Academic Press.Entities:
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Year: 2000 PMID: 10814538 DOI: 10.1006/bbrc.2000.2715
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575