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Purification and characterization of an alpha-macroglobulin proteinase inhibitor from the mollusc Octopus vulgaris.
The cell-free haemolymph of the mollusc Octopus vulgaris inhibited the proteolytic activity of the thermolysin against the high-molecular-mass substrate hide powder azure. The purified inhibitor was a glycoprotein composed of two identical 180 kDa disulphide-linked subunits. In addition to the inhib...
Bewaard in:
| Hoofdauteurs: | , , , , |
|---|---|
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
1992
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1132819/ https://ncbi.nlm.nih.gov/pubmed/1379044 |
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