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KMID : 0380219940270040284
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Journal of Biochemistry and Molecular Biology
1994 Volume.27 No. 4 p.284 ~ p.289
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Isolation and Characterization of a Protease Inhinitor from Drosophila melanogaster
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Abstract
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Abstract:
@EN A trypsin inhibitor was purified 4,100-fold to apparent homogeneity from Drosophila melanogaster. The molecular weight of the purified protein inhibitor was estimated to be 8,000 daltons by gel permeation chromatography, and 8,500 daltons by
sodium
dodesyl sulfate-polyacrylamide gel electrophoresis. The inhibitor froms a complex with bovine pancreatic trypsin at a molar ratio of 1:1. This protein can inhibit other proteases, such as porcine pancreatic elastase and collagenase, but not
chymotrysin,
subtilisin, papain, or pepsin. The inhibitor retained its activity over a broad range of pH(1 to 12) and was relatively thermostable.
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KEYWORD
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