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- W2337696987 abstract "The present study was conducted to study the stability of autolyzed μ-calpain activity and determine whether measurement of μ-calpain activity after anion exchange chromatography accurately reflects its activity in postmortem muscle. Ionic strength and pH affected the stability of partially autolyzed μ-calpain. Complete loss of activity was observed as a result of binding of autolyzed μ-calpain to DEAE-Sephacel when the large subunit of μ-calpain was autolyzed from 80 to 76 kDa. Therefore, determination of μ-calpain by standard anion exchange chromatography may underestimate μ-calpain activity in postmortem muscle. The activity of autolyzed μ-calpain was stabilized by inclusion of glycerol in the buffers, and this permitted us to investigate whether the apparent loss of μ-calpain activity in postmortem muscle is an artifact of the methodology. Despite the inclusion of glycerol in the buffers, a decrease in μ-calpain activity was observed during postmortem storage of muscle, even though the autolyzed enzyme was readily detectable by Western blotting in muscle extracts and column eluates. This result indicates that instability of autolyzed μ-calpain is a major cause for the decline in μ-calpain activity in postmortem muscle." @default.
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- W2337696987 date "2000-01-01" @default.
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- W2337696987 title "Ionic strength-induced inactivation of mu-calpain in postmortem muscle." @default.
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- W2337696987 doi "https://doi.org/10.2527/2000.7892336x" @default.
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