Abstract
The catalytic subunit of protein phosphatase-1 (PP1) isolated from rabbit liver had the same electrophoretic mobility as, and yielded peptide maps identical to those of the 33 kDa form of rabbit skeletal muscle PP1. The predicted amino-acid sequences of PP1 obtained from three rabbit liver cDNA clones were identical to that of PP1α from rabbit skeletal muscle. These findings suggest that the distinctive substrate specificities and regulatory properties of hepatic and skeletal muscle type-1 protein phosphatases are not conferred by the catalytic subunits themselves, but by regulatory subunits that are complexed to the catalytic subunits in vivo.
Original language | English |
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Pages (from-to) | 125-128 |
Number of pages | 4 |
Journal | BBA - Gene Structure and Expression |
Volume | 1008 |
Issue number | 1 |
DOIs | |
Publication status | Published - 1 Jun 1989 |
Keywords
- (Rabbit liver)
- Amino acid sequence
- cDNA cloning
- Nucleic acid sequence
- Peptide mapping
- Protein phosphatase
ASJC Scopus subject areas
- Structural Biology
- Biophysics
- Biochemistry
- Genetics