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The calpain system.
- D. E. Goll, ValeryY F Thompson, Hongqi Li, W. Wei, J. Cong
- Physics, Medicine
- Physiological reviews
- 1 July 2003
The calpain system originally comprised three molecules: two Ca2+-dependent proteases, mu-calpain and m-calpain, and a third polypeptide, calpastatin, whose only known function is to inhibit the two… Expand
The role of autolysis in activity of the Ca2+-dependent proteinases (mu-calpain and m-calpain).
- J. Cong, D. E. Goll, A. M. Peterson, H. P. Kapprell
- Chemistry, Medicine
- The Journal of biological chemistry
- 15 June 1989
A recent hypothesis suggests that proteolytic activity of the micromolar and millimolar Ca2+-requiring forms of the Ca2+-dependent proteinases (mu- and m-calpain, respectively) is regulated in vivo… Expand
A BODIPY fluorescent microplate assay for measuring activity of calpains and other proteases.
The use of 4,4-difluoro-5,7-dimethyl-4-bora-3a, 4a-diaza-s-indacene-3-propionic acid (BODIPY-FL) labeled casein in autoquenching assays of proteolytic activity has been recently described, and we… Expand
Site-directed mutagenesis of colicin E1 provides specific attachment sites for spin labels whose spectra are sensitive to local conformation.
Colicin E1 is an E. coli plasmid-encoded water-soluble protein that spontaneously inserts into lipid membranes to form a voltage-gated ion channel. We have employed a novel approach in which… Expand
Immunoaffinity purification of calpastatin and calpastatin constructs.
- W. Wei, Hongqi Li, J. Cong, V. Thompson, D. E. Goll
- Biology, Medicine
- Biochimica et biophysica acta
- 20 May 2002
It has been difficult to purify calpastatin without using a step involving heating to 90-100 degrees C. Preparations of calpastatin obtained after heating often contain several polypeptides that have… Expand
Localization of the Ca2+‐dependent proteinases and their inhibitor in normal, fasted, and denervated rat skeletal muscle
Immunofluorescence and immunogold localization studies show that the two Ca2+‐dependent proteinases (μ‐calpain for the micromolar Ca2+‐requiring proteinase and m‐calpain for the millimolar… Expand
Localization of the Ca(2+)-dependent proteinases and their inhibitor in normal, fasted, and denervated rat skeletal muscle.
- T. Kumamoto, W. C. Kleese, J. Cong, D. E. Goll, P. Pierce, R. Allen
- The Anatomical record
Immunofluorescence and immunogold localization studies show that the two Ca(2+)-dependent proteinases (mu-calpain for the micromolar Ca(2+)-requiring proteinase and m-calpain for the millimolar… Expand
Effect of monoclonal antibodies specific for the 28-kDa subunit on catalytic properties of the calpains.
Nine monoclonal antibodies (mAbs) specific for the 28-kDa subunit common to mu- and m-calpains have been assayed for their effects on mu- and m-calpains. All nine react with the COOH-terminal part… Expand
The calpain system in human placenta.
The calpain system is involved in a number of human pathologies ranging from the muscular dystrophies to Alzheimer's disease. It is important, therefore, to be able to obtain and to characterize both… Expand
Immunoaffinity purification of the calpains.
A monoclonal antibody to the small subunit common to both mu- and m-calpains can be used in an immunoaffinity column to purify either mu- or m-calpain in a proteolytically active form. Extracts in… Expand