Preferential degradation of the KMnO4-oxidized or N-ethylmaleimide-modified form of sarcoplasmic reticulum ATPase by calpain from chick skeletal muscle.

KMnO4 and N-ethylmaleimide at low concentrations (i.e., below 0.2 and 1.5 mM, respectively) are known to interact specifically with four to five sulfhydryl residues per Ca2+/Mg2(+)-ATPase molecule in sarcoplasmic reticulum. Purified calpain preferentially hydrolyzes the ATPase that was treated with either agent but not the native form of the enzyme. Exposure to each agent with increasing concentrations results in a greater loss of the ATPase activity and renders the enzyme more susceptible to calpain. In addition, beta,r-methylene-ATP, when added during the treatment of KMnO4 or N-ethylmaleimide, can partially protect the ATPase against the degradation. These results suggest that the covalent modification at the specific sulfhydryl residues in sarcoplasmic reticulum ATPase may mark the enzyme for degradation by intracellular proteinases, such as calpain.