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Functional domain of caldesmon
Author(s) -
Szpacenko Adam,
Dąbrowska Renata
Publication year - 1986
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(86)80683-4
Subject(s) - caldesmon , calmodulin , proteolysis , chymotrypsin , cleavage (geology) , chemistry , biochemistry , actin , biophysics , calmodulin binding proteins , biology , trypsin , enzyme , paleontology , fracture (geology)
Limted proteolysis of caldesmon has been used in studying the structure‐function relationship of this protein. Digestion with α‐chymotrypsin yields three major fragments of 110, 80 and 40 kDa. Only the 40 kDa fragment preserves functional properties of the parent molecule: it binds to F‐actin, causes inhibition of actomyosin ATPase and binds to calmodulin in a Ca 2+ ‐dependent manner. Its further degradation produces an 18 kDa polypeptide that also retains all these properties. Neither F‐actin nor calmodulin binding induces dramatic changes in susceptibility to chymotryptic cleavage and the sites of cleavage of caldesmon.