title: Purification and characterization of the trypsin inhibitor from Cucurbita pepo var. patissonina fruits.
abstract: Three trypsin inhibitor fractions were found in white bush fruits (Cucurbita pepo L. var. patissonina). One of them, CPPTI-fIII, was purified to homogeneity by means of affinity and ion exchange chromatography. It is a cysteine-poor protein with an approximate Mr of 21 000. The inhibitor contains arginine at position P1 of the reactive site and inhibits bovine trypsin, hog pancreatic kallikrein and subtilisin. This inhibitor differs from the inhibitors of white bush dormant seeds, CPPTI-I and CPPTI-II, in its amino-acid composition, molecular mass, amino-acid residue at position P1 of the reactive site and inhibition spectrum.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000032:analysis; D008970:Molecular Weight; D010940:Plant Proteins / Q000032:analysis; D010944:Plants / Q000032:analysis*; D013305:Streptomyces griseus / Q000201:enzymology; D014361:Trypsin Inhibitors / Q000302:isolation & purification*
chemical_list: D000596:Amino Acids; D010940:Plant Proteins; D014361:Trypsin Inhibitors; D010450:Endopeptidases