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• W2070091947 startingPage "485" @default.
• W2070091947 abstract "Three proteinase inhibitors have so far been isolated and purified from crayfish haemolymph. One of these, isolated from crayfish plasma, namely a trypsin inhibitor with a molecular mass of 155 kDa was found to inhibit a serine proteinase, ppA, which is involved in the activation of prophenoloxidase, and is localized in the haemocytes. Another high molecular mass proteinase inhibitor, an α2-macroglobulin from crayfish plasma, which is a dimer of 190 kDa-subunits, was only inhibitory towards ppA to a lesser extent. A 23 kDa subtilisin inhibitor, purified from haemocytes, did not have any effect on the serine proteinase. We suggest that mainly the trypsin inhibitor, but to some extent also the α2-macroglobulin, are important in the regulation of the prophenoloxidase activating cascade, as they both inhibit ppA, which in its active form has been shown to mediate prophenoloxidase activation." @default.
• W2070091947 created "2016-06-24" @default.
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• W2070091947 date "1990-01-01" @default.
• W2070091947 modified "2023-10-15" @default.
• W2070091947 title "The effect of endogeneous proteinase inhibitors on the prophenoloxidase activating enzyme, a serine proteinase from crayfish haemocytes" @default.
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• W2070091947 doi "https://doi.org/10.1016/0020-1790(90)90030-x" @default.
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