Mammalian calponin

FEBS Letters

Gimona, Mario¹  Strasser, Peter¹  Small, J.Victor¹  Moessler, Herbert¹  Herzog, Monika¹ 

[1] Institute of Molecular Biology of the Austrian Academy of Sciences, Billrothstraße 11, A-5020 Salzburg, Austria

关键词: Smooth muscle;    Calponin;    Actin-binding protein;    Bacterial expression;    PCR;    polymerase chain reaction;    SDS;    sodium dodecyl sulfate;    pI;    isoelectric point;   

DOI  :  10.1016/0014-5793(93)80909-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown