Skip to main content
construction release_alert
Scholars@Duke will be undergoing maintenance April 11-15. Some features may be unavailable during this time.
cancel

Specificity of alpha 2-macroglobulin covalent cross-linking for the active domain of proteinases.

Publication ,  Journal Article
Pizzo, SV; Rajagopalan, S; Roche, PA; Fuchs, HE; Feldman, SR; Gonias, SL
Published in: Biol Chem Hoppe Seyler
November 1986

The reaction of alpha 2-macroglobulin (alpha 2M) with the two-chain enzyme plasma kallikrein results in covalent bond formation between the catalytic subunit and the inhibitor. We have recently published a model of alpha 2M which suggests that this phenomenon may be a general mechanism when multisubunit proteinases are inactivated by alpha 2M. In order to test this hypothesis, we studied the reactions of factor Xa, plasmin, streptokinase-plasmin and alpha-thrombin with alpha 2M. In the case of factor Xa the catalytic heavy chain demonstrated greater than 99% covalent incorporation while over 97% of the light chain failed to crosslink to the inhibitor. Preferential binding of the catalytic light chains of plasmin (70% covalent incorporation) and plasmin in complex with streptokinase (79% covalent incorporation) was also observed. Finally, 82% covalent incorporation of the catalytic heavy chain of alpha-thrombin was found. These studies demonstrate that in the case of multisubunit proteinases, the chain containing the active site demonstrates preferential binding as predicted by the model supporting placement of the site of covalent binding close to the "bait region" of alpha 2M.

Duke Scholars

Published In

Biol Chem Hoppe Seyler

DOI

ISSN

0177-3593

Publication Date

November 1986

Volume

367

Issue

11

Start / End Page

1177 / 1182

Location

Germany

Related Subject Headings

  • alpha-Macroglobulins
  • Thrombin
  • Protein Binding
  • Peptide Hydrolases
  • Humans
  • Fibrinolysin
  • Factor X
  • Electrophoresis, Polyacrylamide Gel
  • Cross-Linking Reagents
  • Binding Sites
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Pizzo, S. V., Rajagopalan, S., Roche, P. A., Fuchs, H. E., Feldman, S. R., & Gonias, S. L. (1986). Specificity of alpha 2-macroglobulin covalent cross-linking for the active domain of proteinases. Biol Chem Hoppe Seyler, 367(11), 1177–1182. https://doi.org/10.1515/bchm3.1986.367.2.1177
Pizzo, S. V., S. Rajagopalan, P. A. Roche, H. E. Fuchs, S. R. Feldman, and S. L. Gonias. “Specificity of alpha 2-macroglobulin covalent cross-linking for the active domain of proteinases.Biol Chem Hoppe Seyler 367, no. 11 (November 1986): 1177–82. https://doi.org/10.1515/bchm3.1986.367.2.1177.
Pizzo SV, Rajagopalan S, Roche PA, Fuchs HE, Feldman SR, Gonias SL. Specificity of alpha 2-macroglobulin covalent cross-linking for the active domain of proteinases. Biol Chem Hoppe Seyler. 1986 Nov;367(11):1177–82.
Pizzo, S. V., et al. “Specificity of alpha 2-macroglobulin covalent cross-linking for the active domain of proteinases.Biol Chem Hoppe Seyler, vol. 367, no. 11, Nov. 1986, pp. 1177–82. Pubmed, doi:10.1515/bchm3.1986.367.2.1177.
Pizzo SV, Rajagopalan S, Roche PA, Fuchs HE, Feldman SR, Gonias SL. Specificity of alpha 2-macroglobulin covalent cross-linking for the active domain of proteinases. Biol Chem Hoppe Seyler. 1986 Nov;367(11):1177–1182.

Published In

Biol Chem Hoppe Seyler

DOI

ISSN

0177-3593

Publication Date

November 1986

Volume

367

Issue

11

Start / End Page

1177 / 1182

Location

Germany

Related Subject Headings

  • alpha-Macroglobulins
  • Thrombin
  • Protein Binding
  • Peptide Hydrolases
  • Humans
  • Fibrinolysin
  • Factor X
  • Electrophoresis, Polyacrylamide Gel
  • Cross-Linking Reagents
  • Binding Sites