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Title: Purification of a latent protein phosphatase from rabbit skeletal muscle
Authors: Yang, Shiaw-Der ×
Vandenheede, Jackie
Merlevede, Wilfried #
Issue Date: Apr-1984
Series Title: Biochemical and Biophysical Research Communications vol:118 issue:3 pages:923-8
Abstract: A high molecular weight protein phosphatase (Mr = 260K) has been isolated from rabbit skeletal muscle. The enzyme has a very low activity towards phosphorylase a isolated from the same tissue, but its activity towards this substrate is stimulated several fold after dissociation by 2-mercaptoethanol treatment. The purified phosphatase shows one major protein staining band on non denaturing polyacrylamide gel electrophoresis, and contains four subunits with molecular weights of 95K, 75K, 65K and 38K. The catalytic activity resides in the Mr = 38K subunit and is not sensitive to inhibition by the heat stable protein phosphatase inhibitor-1 or modulator protein. Polyamines stimulate the holoenzyme in a dose dependent, biphasic manner, but inhibit the activity of the dissociated Mr = 38K catalytic subunit.
URI: 
ISSN: 0006-291X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biochemistry Section (Medicine) (-)
× corresponding author
# (joint) last author

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