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Limited proteolysis of pig liver CoA synthase: evidence for subunit identity
Author(s) -
Worrall D.Margaret,
Lambert Sarah F.,
Tubbs Philip K.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81258-8
Subject(s) - proteolysis , protein subunit , atp synthase , biochemistry , enzyme , trypsin , chemistry , gel electrophoresis , dimer , biology , microbiology and biotechnology , gene , organic chemistry
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.