Purification and properties of a protease inhibitor from crayfish hemolymph |
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Authors: | Lena Häll Kenneth Söderhäll |
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Affiliation: | Institute of Physiological Botany, University of Uppsala, Box 540, S-751 21 Uppsala, Sweden |
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Abstract: | A protease inhibitor from the hemolymph of crayfish, Astacus astacus, has been purified by differential centrifugation, acid precipitation and preparative isoelectric focusing. The inhibitor was apparent homogenous in SDS-electrophoresis and had a molecular weight of 23,000. pI was determined to be 4.7 by isoelectric focusing. No inhibitory activity was lost when the inhibitor was incubated in a pH range of 1–11.5. The purified inhibitor was heat stable. Urea (6 m) had no effect upon the inhibitor. The inhibitor was active against subtilisin and a partly purified protease from the fungus Aphanomyces astaci. Pronase was slightly inhibited whereas trypsin, chymotrypsin, papain, Arthrobacter protease, and extracellular proteases from the fungi Aphanomyces stellatus and A. laevis were unaffected. The importance of protease inhibitors in pathogenesis between the parasitic fungus, A. astaci, and its crayfish host, A. astacus is discussed. |
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Keywords: | hemocytes purification of protease inhibitors subtilisin inhibitor inhibition of fungal protease role in defense |
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