Purification and characterization of a calcium-dependent protease from rat liver
- 1 December 1983
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 22 (26), 6287-6291
- https://doi.org/10.1021/bi00295a038
Abstract
A Ca-dependent protease, previously identified in rat liver and designated peak II, was purified and characterized. The Ca-dependent proteolytic activity was accounted for by an 80,000-dalton protein. Depending on the method of purification, this protease could be associated with a 28,000-dalton subunit, which was devoid of protease activity. The catalytic characteristics of the 2 different forms of the protease were indistinguishable. Each was half-maximally activated by .apprx. 250 .mu.M Ca.This publication has 13 references indexed in Scilit:
- Rabbit skeletal muscle calcium-dependent protease requiring millimolar CA2+. Purification, subunit structure, and Ca2+-dependent autoproteolysis.Journal of Biological Chemistry, 1982
- Silver staining of proteins in polyacrylamide gelsAnalytical Biochemistry, 1981
- Studies on the Ca2+-Activated Neutral Proteinase of Rabbit Skeletal Muscle. I. The Characterization of the 80 K and the 30 K SubunitsThe Journal of Biochemistry, 1981
- A new method for the preparation of a calcium activated neutral protease highly sensitive to calcium ionsBiochemical and Biophysical Research Communications, 1981
- A calcium-activated protease possibly involved in myofibrillar protein turnover. Isolation of a low-calcium-requiring form of the proteaseBiochimica et Biophysica Acta (BBA) - Enzymology, 1981
- Purification and some physico-chemical and enzymic properties of a calcium ion-activated neutral proteinase from rabbit skeletal muscleBiochemical Journal, 1979
- Identification of two protease inhibitors from bovine cardiac muscle.Journal of Biological Chemistry, 1978
- Studies of a Calcium-Activated Neutral Protease from Chicken Skeletal MuscleThe Journal of Biochemistry, 1978
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresisArchives of Biochemistry and Biophysics, 1968