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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...

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Autors principals: Thøgersen, I B, Salvesen, G, Brucato, F H, Pizzo, S V, Enghild, J J
Format: Artigo
Idioma:Inglês
Publicat: 1992
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC1132819/
https://ncbi.nlm.nih.gov/pubmed/1379044
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