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PMID: 1312807 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Expression and turnover of acylphosphatase (muscular isoenzyme) in L6 myoblasts during myogenesis.

Archives of biochemistry and biophysics ·Vol. 294 ·No. 1 ·1992-04-00 ·Pages 261-4

Berti A, Degl'Innocenti D, Stefani M, Ramponi G

Abstract

Acylphosphatase (muscular isoenzyme) levels have been measured in L6J1 myoblasts either proliferating or differentiating into myotubes. Results indicated that the increase in enzyme levels during differentiation is very similar to that of creatine kinase, a specific muscular enzyme. The half-lives of acylphosphatase in myoblasts and myotubes were also determined; t1/2 values of 3 h 30 min (myoblasts), and 2 h 18 min (myotubes) were found. These results indicate that acylphosphatase could be considered a short-lived muscle-specific protein and that its increase in myotubes must be accompanied by an activation of its breakdown.

MeSH Terms
Acid Anhydride Hydrolases Animals Cell Differentiation Cell Line Enzyme-Linked Immunosorbent Assay Half-Life Isoenzymes/metabolism Kinetics Muscles/cytology,enzymology Phosphoric Monoester Hydrolases/metabolism Rats
Chemicals
Isoenzymes Phosphoric Monoester Hydrolases Acid Anhydride Hydrolases acylphosphatase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Berti A
Department of Biochemical Sciences, University of Florence, Italy.
Degl'Innocenti D
Stefani M
Ramponi G
Article Info
Journal
Archives of biochemistry and biophysics
Abbr.
Arch Biochem Biophys
ISSN
0003-9861
Published
1992-04-00
Pages
261-4
Language
English
Region
United States
NLM ID
0372430
Subset
IM
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