Trypsin inhibitors in summer squash (Cucurbita pepo) seeds. Isolation, purification and partial characterization of three inhibitors.
Three trypsin inhibitors were isolated from summer squash (Cucurbita pepo) seeds and purified to homogeneity by fractionation with ammonium sulphate and methanol, ion-exchange chromatography and gel filtration. All three inhibitors have lysine at their active site. Two of them (II, IV) show the same isoelectric point (at pH 5.6), amino acid composition and molecular mass (3259). The third inhibitor (III) of molecular mass of 3654 and isoelectric point at 4.9 has additionally one histidine residue and two glutamic acid residues more per molecule.
D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D008970:Molecular Weight; D010940:Plant Proteins / Q000032:analysis / Q000302:isolation & purification / Q000494:pharmacology*; D010944:Plants / Q000032:analysis*; D014361:Trypsin Inhibitors / Q000032:analysis / Q000302:isolation & purification / Q000494:pharmacology*
D000596:Amino Acids; D010940:Plant Proteins; D014361:Trypsin Inhibitors; C031809:trypsin inhibitor, Cucurbita sp.