Purification and Characterization of Serine Proteinase Inhibitors from Gourd(Lagenaria leucantha RUSBY var. Gourda MAKINO) Seeds.

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  • Purification and Characterization of Serine Proteinase Inhibitors form Gourd <i>(Lagenaria leucantha</i> R<scp>USBY</scp> var. <i>Gourda</i> M<scp>AKINO</scp>) Seeds

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Gourd seed inhibitors were purified in the following manner : gourd seeds were ground and extracted with 10 mM ammonium carbonate, pH 7.8. The extract was precipitated with 65-90% acetone and the acetone precipitates were gel filtered in a Cellulofine GCL-90-m column. Fractions of 3000 Da showing trypsin inhibitory activity were combined and purified further by ion exchange and reversed phase chromatographies. Three inhibitors, LLTI-I, II, and III were thus purified to homogeneity and the amino acid sequences of these inhibitors were : [table] The exact sequences are unique but very similar to proteinase inhibitors belonging to the squash family. Based on the sequence, it is assumed that the peptide bond (Arg-Ile) found in the three inhibitors is the reactive site for trypsin. The Ki values estimated for complexes of LLTI-I, II. and III with bovine trypsin were 3.6×10-10M, and 3.0×10-11M, respectively.

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