Limited proteolysis of pig liver CoA synthase: evidence for subunit identity.
The bifunctional enzyme CoA synthase can be nicked by trypsin without loss of its activities. The original dimer of subunit Mr approx. 61 000 yields fragments of Mr 41 000 and 22 000 as seen on gel electrophoresis in the presence of SDS, but the nicked enzyme retains the native Mr 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.
D000818:Animals; D003066:Coenzyme A Ligases / Q000302:isolation & purification*; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D010446:Peptide Fragments / Q000302:isolation & purification; D011487:Protein Conformation; D013552:Swine; D014357:Trypsin
D010446:Peptide Fragments; D014357:Trypsin; D003066:Coenzyme A Ligases