Calponin is a smooth muscle specific, actin-, tropomyosin- and calmodulin-binding protein thought to be involved in some way in the regulation or modulation of contraction. Here we describe the cloning and bacterial expression of two calponin species from murine and porcine smooth muscle tissues. Primary and secondary structural analyses of the deduced amino acid sequences revealed a high degree of homology to avian calponin with the exception of a short and variable C-terminal segment. The sequence data demonstrate that the two mammalian calponin variants do not arise via alternative splicing but are encoded by different genes.
Useful keywords (using NLM MeSH Indexing)
Amino Acid Sequence
Electrophoresis, Gel, Two-Dimensional
Molecular Sequence Data
Sequence Homology, Amino Acid
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