Limited proteolysis of pig liver CoA synthase: evidence for subunit identity

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Abstract
The bifunctional enzyme CoA synthase can be nicked by trypsin without loss of its activities. The original dimer of subunit M r approx. 61000 yields fragments of M r 41000 and 22000 as seen on gel electrophoresis in the presence of SDS, but the nicked enzyme retains the native M r of 118 000. Further proteolysis occurs rapidly in the absence of protecting substrates. The N‐terminal of native CoA synthase is proline, and proteolysis exposes glycine as a second N‐terminal. This evidence strongly suggests that the subunits are identical.