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Anomalous electrochemical behavior of clostripain: Evidence for disulfide isolation conformers

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Summary

Purified preparations of clostripain exhibit two distinct components on analytical and preparative acrylamide gel electrophoresis as well as adsorption chromatography on hydroxylapatite. Both components are of identical molecular size and specific activity. By reducing the enzyme for an extended period of time prior to chromatography, the specific activity increases by a factor of four and the enzyme elutes from the hydroxylapatite column as a homogeneous peak. Enzyme labeled at the active site with3H-TLCK exhibits a similar chromatographic behavior to native enzyme on hydroxylapatite.

It is inferred that such behavior may be attributed to a two phase disulfide reduction, one involving reduction of a disulfide thereby freeing an active site SH group and a second disulfide reduction resulting in the chromatographic transition.

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Authors and Affiliations

  1. The Univ. of Tennessee Memorial Res. Center, 37920, Knoxville, Tennessee, USA

    William H. Porter

  2. Dep. of Microbiol. and Med., Vanderbilt Univ. School of Med., 37232, Nashville, Tennessee, USA

    William M. Mitchell

Authors
  1. William H. Porter
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  2. William M. Mitchell
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Porter, W.H., Mitchell, W.M. Anomalous electrochemical behavior of clostripain: Evidence for disulfide isolation conformers. Mol Cell Biochem 1, 95–99 (1973). https://doi.org/10.1007/BF01659942

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