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Mammalian calponin
Author(s) -
Strasser Peter,
Gimona Mario,
Moessler Herbert,
Herzog Monika,
Small J.Victor
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80909-e
Subject(s) - calponin , actin , alternative splicing , calmodulin , tropomyosin , microbiology and biotechnology , biology , cloning (programming) , homology (biology) , gene , chemistry , biochemistry , exon , computer science , programming language , enzyme
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.