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

FEBS Letters

Lambert, Sarah F.¹  Worrall, D.Margaret¹  Tubbs, Philip K.¹ 

[1] Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 IQW, England

关键词: CoA synthase;    Limited proteolysis;    N-terminal analysis;    Subunit identity;    TPCK;    1-tosylamide-2-phenylethyl chloromethyl ketone;    DABITC;    dimethylaminoben-zene-4-isothiocyanate;    PITC;    phenylisothiocyanate;   

DOI  :  10.1016/0014-5793(85)81258-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown