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Proteolysis of liver plectin by mu-calpain
M Muenchbach1, M Dell'Ambrogio, P Gazzotti
1Laboratory of Biochemistry III, Swiss Federal Institute of Technology (ETH), Zurich, CH-8092, Switzerland.
Biochemical and Biophysical Research Communications
|August 26, 1998
Abstract:
Rat liver plectin was found to be mainly associated with plasma membrane fractions enriched in junctional complexes. The membrane-associated plectin has been partially isolated. Plectin co-purifies with a 200 kDa polypeptide which, on the basis of sequence homology, has been identified as a myosin like-protein. The interaction of mu-calpain with liver plectin has been investigated. Plectin is very sensitive to mu-calpain and is digested to give a fragment of 240 kDa.