Et Blopjiyslca ~ta Elsevier

نویسندگان

  • Kadee J Raser
  • Michelle Buroker-Kilgore
  • Kevin K W Wang
چکیده

Human JL-calpain is activated maximally by 100-200 JLM Ca2+. Both the 80 kDa and 29 kDa subunits of JL-calpain have a EF-hand type calcium-binding domain. It is known that trivalent terbium ion (Tb3+) mimics Ca2+ in many biological systems. We found that Tb3+ alone transiently activated calpain. However, in the presence of Ca2+ , Tb3+ inhibited JL-calpain with an IC5o of about loo JLM. As high as 10 mM Ca2+ did not significantly shift the IC5o of Tb3+. Preincubating JL-calpain by Ca2+ (before Tb3+ and substrate were added) did not diniinish the inhibition by Tb3+. On the other hand, pretreating JL-calpain with Tb3+ produced that Tb3+ has a slow dissociation rate for the calcium-binding sites when compared to Ca2+. Electrophoretic analysis revealed that terbium ion transiently activated JL-calpain followed by the aggregation of the proteinase.

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تاریخ انتشار 1995