| Literature DB >> 2668328 |
J Bryan1.
Abstract
Recent estimates of molecular weight and cDNA sequencing indicate that smooth muscle caldesmons are considerably smaller than previously thought. The anomalous behaviour of these proteins during SDS-polyacrylamide gel electrophoresis can be correlated with their high acidic amino acid content. The results suggest a need to re-evaluate the stoichiometric relations of caldesmon to tropomyosin and actin in thin filaments and its presumed 1:1 interaction with calmodulin.Entities:
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Year: 1989 PMID: 2668328 DOI: 10.1007/bf01739964
Source DB: PubMed Journal: J Muscle Res Cell Motil ISSN: 0142-4319 Impact factor: 2.698