Arginine-specific ADP-ribosyltransferase from rabbit skeletal muscle sarcoplasmic reticulum is solubilized as the active form with trypsin: Partial purification and characterization
- 1 October 1989
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 164 (1) , 128-133
- https://doi.org/10.1016/0006-291x(89)91692-6
Abstract
No abstract availableFunding Information
- Ministry of Education, Culture, Sports, Science and Technology
This publication has 10 references indexed in Scilit:
- Endogenous ADP-ribosylation in skeletal muscle membranesArchives of Biochemistry and Biophysics, 1988
- ADP-ribosylation of Ca2+-dependent ATPase In vitro suppresses the enzyme activityBiochemical and Biophysical Research Communications, 1987
- Mono(ADP-ribosyl)ation of Ca2+-dependent ATPase in rabbit skeletal muscle sarcoplasmic reticulum and the effect of poly L-lysineBiochemical and Biophysical Research Communications, 1987
- Determination of ADP-ribosyl arginine anomers by reverse-phase high-performance liquid chromatographyAnalytical Biochemistry, 1986
- NAD: Guanidino group specific mono ADP-ribosyltransferase activity in skeletal muscleBiochemical and Biophysical Research Communications, 1984
- ADP-ribosyltransferase from hen liver nuclei. Purification and characterization.Journal of Biological Chemistry, 1984
- Mono(ADP-ribosyl)ation of hen liver nuclear proteins suppresses phosphorylationBiochemical and Biophysical Research Communications, 1983
- Histone-dependent and histone-independent forms of an ADP-ribosyltransferase from human and turkey erythrocytes.Proceedings of the National Academy of Sciences, 1981
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976