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Sodium dodecyl sulfate-stable complexes between serpins and active or inactive proteinases contain the region COOH-terminal to the reactive site loop.

Publication ,  Journal Article
Christensen, S; Valnickova, Z; Thøgersen, IB; Pizzo, SV; Nielsen, HR; Roepstorff, P; Enghild, JJ
Published in: J Biol Chem
June 23, 1995

Recently inhibitors of the serpin family were shown to form complexes with dichloroisocoumarine (DCI)-inactivated proteinases under native conditions (Enghild, J. J., Valnickova, Z., Thøgersen I., and Pizzo, S. V. (1994) J. Biol. Chem. 269, 20159-20166). This study demonstrates that serpin-DCI/proteinase complexes resist dissociation when analyzed in reduced SDS-polyacrylamide gel electrophoresis. Previously, SDS-stable serpin-proteinase complexes have been observed only between serpins and catalytically active proteinases. The stability of these complexes is believed to result from an acyl-ester bond between the active site Ser195 of the proteinase and the alpha-carbonyl group of the scissile bond in the reactive site loop. We have further analyzed the structure of the SDS-stable serpin-proteinase and serpin-DCI/proteinase complexes. The results of these studies demonstrate the presence of the COOH-terminal region of the serpin in both complexes. Since (i) modification of Ser195 does not prevent formation of SDS-stable complexes and (ii) COOH-terminal peptides are present in both complexes, the previously described mechanism does not sufficiently explain the formation of SDS-stable complexes.

Duke Scholars

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

June 23, 1995

Volume

270

Issue

25

Start / End Page

14859 / 14862

Location

United States

Related Subject Headings

  • Trypsin
  • Swine
  • Sodium Dodecyl Sulfate
  • Serpins
  • Serine Proteinase Inhibitors
  • Serine
  • Protein Structure, Secondary
  • Protein Binding
  • Kinetics
  • Isocoumarins
 

Citation

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Christensen, S., Valnickova, Z., Thøgersen, I. B., Pizzo, S. V., Nielsen, H. R., Roepstorff, P., & Enghild, J. J. (1995). Sodium dodecyl sulfate-stable complexes between serpins and active or inactive proteinases contain the region COOH-terminal to the reactive site loop. J Biol Chem, 270(25), 14859–14862. https://doi.org/10.1074/jbc.270.25.14859
Christensen, S., Z. Valnickova, I. B. Thøgersen, S. V. Pizzo, H. R. Nielsen, P. Roepstorff, and J. J. Enghild. “Sodium dodecyl sulfate-stable complexes between serpins and active or inactive proteinases contain the region COOH-terminal to the reactive site loop.J Biol Chem 270, no. 25 (June 23, 1995): 14859–62. https://doi.org/10.1074/jbc.270.25.14859.
Christensen S, Valnickova Z, Thøgersen IB, Pizzo SV, Nielsen HR, Roepstorff P, et al. Sodium dodecyl sulfate-stable complexes between serpins and active or inactive proteinases contain the region COOH-terminal to the reactive site loop. J Biol Chem. 1995 Jun 23;270(25):14859–62.
Christensen, S., et al. “Sodium dodecyl sulfate-stable complexes between serpins and active or inactive proteinases contain the region COOH-terminal to the reactive site loop.J Biol Chem, vol. 270, no. 25, June 1995, pp. 14859–62. Pubmed, doi:10.1074/jbc.270.25.14859.
Christensen S, Valnickova Z, Thøgersen IB, Pizzo SV, Nielsen HR, Roepstorff P, Enghild JJ. Sodium dodecyl sulfate-stable complexes between serpins and active or inactive proteinases contain the region COOH-terminal to the reactive site loop. J Biol Chem. 1995 Jun 23;270(25):14859–14862.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

June 23, 1995

Volume

270

Issue

25

Start / End Page

14859 / 14862

Location

United States

Related Subject Headings

  • Trypsin
  • Swine
  • Sodium Dodecyl Sulfate
  • Serpins
  • Serine Proteinase Inhibitors
  • Serine
  • Protein Structure, Secondary
  • Protein Binding
  • Kinetics
  • Isocoumarins