Purification and properties of rabbit liver cathepsin M and cathepsin B
- 1 November 1985
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 243 (1) , 46-61
- https://doi.org/10.1016/0003-9861(85)90772-6
Abstract
No abstract availableThis publication has 39 references indexed in Scilit:
- Amino acid sequence of human liver cathepsin BFEBS Letters, 1985
- Inactivation of Rabbit Liver and Muscle Aldolases by Limited Proteolysis by Lysosomal Cathepsin MCurrent Topics in Cellular Regulation, 1985
- Binding of monoclonal antibody to cathepsin M located on the external surface of rabbit lysosomesArchives of Biochemistry and Biophysics, 1984
- Localization of two lysosomal proteinases on the external surface of the lysosomal membraneBiochemical and Biophysical Research Communications, 1982
- Cathepsin M: A lysosomal proteinase with aldolase-inactivating activityArchives of Biochemistry and Biophysics, 1982
- Limited proteolysis of liver and muscle aldolases: Effects of subtilisin, cathepsin B, and Staphylococcus aureus proteaseArchives of Biochemistry and Biophysics, 1982
- Inactivation of liver aldolase in fasting rabbits: Evidence for the accumulation of two different immunoreactive formsArchives of Biochemistry and Biophysics, 1980
- Degradation of fructose-1,6-bisphosphate aldolase by cathepsin BBiochemical Journal, 1980
- Evidence for an interaction between fructose 1,6-bisphosphatase and fructose 1,6-bisphosphate aldolaseArchives of Biochemistry and Biophysics, 1979
- The limited proteolysis of rabbit muscle aldolase by cathepsin B1Biochemical and Biophysical Research Communications, 1978