A catalytic subunit of calpain possesses full proteolytic activity.
Previous studies on the refolding of calpain, a heterodimer comprising a catalytic 80 kDa subunit and a regulatory 30 kDa subunit, indicate that both subunits are required for the expression of full protease activity. We reexamined the conditions for refolding of calpain and found that under optimized conditions the renatured 80 kDa subunit has full enzyme activity even in the absence of the 30 kDa subunit. The 30 kDa subunit stabilizes the 80 kDa subunit rather than enhancing its activity. The theory that calpain functions as a dimer requires reexamination.
Yoshizawa
T
T
Department of Molecular Biology, University of Tokyo, Japan.
Sorimachi
H
H
Tomioka
S
S
Ishiura
S
S
Suzuki
K
K
D001426:Bacterial Proteins / Q000494:pharmacology; D002154:Calpain / Q000737:chemistry / Q000378:metabolism*; D018833:Chaperonins; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins / Q000494:pharmacology; D011092:Polyethylene Glycols; D011489:Protein Denaturation; D017510:Protein Folding
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C028715:GroE protein, E coli; D006360:Heat-Shock Proteins; D011092:Polyethylene Glycols; D002154:Calpain; D018833:Chaperonins