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Evidence for a role of sulfhydryl groups in catalytic activity and subunit interaction of the cyclic GMP-dependent protein kinase from silkworm.

Authors
  • Rochette-Egly, C
  • Castagna, M
Type
Published Article
Journal
Biochimica et Biophysica Acta
Publisher
Elsevier
Publication Date
Sep 11, 1978
Volume
526
Issue
1
Pages
107–115
Identifiers
PMID: 210822
Source
Medline
License
Unknown

Abstract

Guanosine 3':5'-monophosphate-dependent protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37) has been isolated from silkworm pupal fat body (Bombyx mori) which is devoid of any adenosine 3':5'-monophosphate-dependent protein kinase. The enzyme displayed catalytic properties which were roughly similar to those described for adenosine 3':5'-monophosphate-dependent protein kinase. This similarity has been found in substrate specificity, optimal Mg2+ dependency, polyamines effects and the lack of dependency upon sulfhydryl compound for activation by cyclic GMP. Treatment of the enzyme with sulfhydryl reagents, N-ethylmaleimide or p-chloromercuribenzoic acid, inhibited the catalytic activity as well as the dissociation of the binding and catalytic activities as shown by means of sucrose-density gradient ultracentrifugation. In the presence of cyclic GMP or histone, the disulfide-linked structure did not dissociate into separate subunits nor did it migrate as the holoenzyme but sedimented as an intermediate form carrying both binding and catalytic activities.

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