Demonstration of two distinct high molecular weight proteases in rabbit reticulocytes, one of which degrades ubiquitin conjugates.
Open Access
- 1 February 1987
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 262 (6), 2451-2457
- https://doi.org/10.1016/s0021-9258(18)61525-x
Abstract
No abstract availableThis publication has 64 references indexed in Scilit:
- Effects of denaturation and methylation on the degradation of proteins in cultured hepatoma cells and in reticulocyte cell‐free systemsEuropean Journal of Biochemistry, 1985
- Relevance of protease “inhibitor” to the ATP-ubiquitin proteolytic systemBiochemical and Biophysical Research Communications, 1984
- Identification of three high molecular mass cysteine proteinases from rat skeletal muscleFEBS Letters, 1983
- A high-molecular-weight cysteine endopeptidase from rat skeletal muscleBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Role for the Adenosine Triphosphate-Dependent Proteolytic Pathway in Reticulocyte MaturationScience, 1982
- Cation‐Sensitive Neutral Endopeptidase: Isolation and Specificity of the Bovine Pituitary EnzymeJournal of Neurochemistry, 1980
- Determination and Characteristics of Energy-Dependent Proteolysis in Rabbit ReticulocytesEuropean Journal of Biochemistry, 1980
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Physicochemical properties of rabbit skeletal muscle phosphorylase kinaseBiochemistry, 1973
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970