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Purification and characterization of α2-, α2-β- and β-macroglobulin inhibitors in the hedgehog, Erinaceus europaeus : β-macroglobulin identified as the plasma antihemorrhagic factor

de Wit, Cynthia A. and Weström, Björn R. LU (1987) In Toxicon 25(11). p.1209-1219
Abstract

C. A. de Wit and B. R. Weström. Purification and characterization of α2-, α2-β- and β-macroglobulin inhibitors in the hedgehog, Erinaceus europaeus: β-macroglobulin identified as the plasma antihemorrhagic factor. Toxicon 25, 1209 - 1219, 1987. - Three macroglobulin inhibitors were purified from hedgehog (Erinaceus europaeus) plasma by sequential chromatography on Cibacron Blue Sepharose, Sephacryl S-200 and preparative agarose gel electrophoresis. Each macroglobulin was characterized for proteinase inhibiting activity, molecular weight by polyacrylamide gel electrophoresis (PAGE), subunit size by sodium dodecyl sulfate (SDS)-PAGE, immunological cross-reactivity to other macroglobulins and antihemorrhagic activity... (More)

C. A. de Wit and B. R. Weström. Purification and characterization of α2-, α2-β- and β-macroglobulin inhibitors in the hedgehog, Erinaceus europaeus: β-macroglobulin identified as the plasma antihemorrhagic factor. Toxicon 25, 1209 - 1219, 1987. - Three macroglobulin inhibitors were purified from hedgehog (Erinaceus europaeus) plasma by sequential chromatography on Cibacron Blue Sepharose, Sephacryl S-200 and preparative agarose gel electrophoresis. Each macroglobulin was characterized for proteinase inhibiting activity, molecular weight by polyacrylamide gel electrophoresis (PAGE), subunit size by sodium dodecyl sulfate (SDS)-PAGE, immunological cross-reactivity to other macroglobulins and antihemorrhagic activity against European viper (Vipera berus) venom. Hedgehog α2-macroglobulin is a tetramer (Mr 800,000) composed of identical monomers (Mr 200,000) that inhibits all proteinases tested and is the homologue of human α2-macroglobulin, rat α2-acute phase globulin, dog α1-macroglobulin and swine α2-macroglobulin fast. Hedgehog α2-β-macroglobulin is a dimer (Mr 450 - 550,000) composed of identical monomers (Mr 200,000) that inhibits all proteinases tested and appears to be structurally similar to other animal ';half-molecule' macroglobulins. Hedgehog β-macroglobulin (Mr 700,000) gave subunits of 34,000 and 39,000 after SDS-PAGE and showed cross-reactivity with swine α2-macroglobulin slow. It inhibits all proteinases tested and is the only macroglobulin with antihemorrhagic activity against V. berus venom. This antihemorrhagic activity may be due to β-macroglobulin's different structure as compared to other macroglobulins, which may make it less susceptible to inactivation by venom proteinases.

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Toxicon
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25
issue
11
pages
11 pages
publisher
Elsevier
external identifiers
  • pmid:3124298
  • scopus:0023475808
ISSN
0041-0101
DOI
10.1016/0041-0101(87)90139-5
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English
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581886e3-81d5-4c66-9223-a50833d66c8b
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@article{581886e3-81d5-4c66-9223-a50833d66c8b,
  abstract     = {{<p>C. A. de Wit and B. R. Weström. Purification and characterization of α<sub>2</sub>-, α<sub>2</sub>-β- and β-macroglobulin inhibitors in the hedgehog, Erinaceus europaeus: β-macroglobulin identified as the plasma antihemorrhagic factor. Toxicon 25, 1209 - 1219, 1987. - Three macroglobulin inhibitors were purified from hedgehog (Erinaceus europaeus) plasma by sequential chromatography on Cibacron Blue Sepharose, Sephacryl S-200 and preparative agarose gel electrophoresis. Each macroglobulin was characterized for proteinase inhibiting activity, molecular weight by polyacrylamide gel electrophoresis (PAGE), subunit size by sodium dodecyl sulfate (SDS)-PAGE, immunological cross-reactivity to other macroglobulins and antihemorrhagic activity against European viper (Vipera berus) venom. Hedgehog α<sub>2</sub>-macroglobulin is a tetramer (M<sub>r</sub> 800,000) composed of identical monomers (M<sub>r</sub> 200,000) that inhibits all proteinases tested and is the homologue of human α<sub>2</sub>-macroglobulin, rat α<sub>2</sub>-acute phase globulin, dog α<sub>1</sub>-macroglobulin and swine α<sub>2</sub>-macroglobulin fast. Hedgehog α<sub>2</sub>-β-macroglobulin is a dimer (M<sub>r</sub> 450 - 550,000) composed of identical monomers (M<sub>r</sub> 200,000) that inhibits all proteinases tested and appears to be structurally similar to other animal ';half-molecule' macroglobulins. Hedgehog β-macroglobulin (M<sub>r</sub> 700,000) gave subunits of 34,000 and 39,000 after SDS-PAGE and showed cross-reactivity with swine α<sub>2</sub>-macroglobulin slow. It inhibits all proteinases tested and is the only macroglobulin with antihemorrhagic activity against V. berus venom. This antihemorrhagic activity may be due to β-macroglobulin's different structure as compared to other macroglobulins, which may make it less susceptible to inactivation by venom proteinases.</p>}},
  author       = {{de Wit, Cynthia A. and Weström, Björn R.}},
  issn         = {{0041-0101}},
  language     = {{eng}},
  number       = {{11}},
  pages        = {{1209--1219}},
  publisher    = {{Elsevier}},
  series       = {{Toxicon}},
  title        = {{Purification and characterization of α<sub>2</sub>-, α<sub>2</sub>-β- and β-macroglobulin inhibitors in the hedgehog, Erinaceus europaeus : β-macroglobulin identified as the plasma antihemorrhagic factor}},
  url          = {{http://dx.doi.org/10.1016/0041-0101(87)90139-5}},
  doi          = {{10.1016/0041-0101(87)90139-5}},
  volume       = {{25}},
  year         = {{1987}},
}