Journal article
Proteolysis of liver plectin by mu-calpain.
- Muenchbach M Laboratory of Biochemistry III, Swiss Federal Institute of Technology (ETH), Zurich, CH-8092, Switzerland.
- Dell'Ambrogio M
- Gazzotti P
- 1998-08-26
Published in:
- Biochemical and biophysical research communications. - 1998
Amino Acid Sequence
Animals
Calpain
Cell Membrane
Cyanogen Bromide
Female
Intermediate Filament Proteins
Liver
Molecular Sequence Data
Peptide Fragments
Plectin
Rats
English
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.
- Language
-
- English
- Open access status
- closed
- Identifiers
-
- DOI 10.1006/bbrc.1998.9138
- PMID 9712691
- Persistent URL
- https://sonar.ch/global/documents/123370
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