Aspartyl proteinase from cucumber (Cucumis sativus) seeds. Preparation and characteristics.
Aspartyl proteinase (EC 3.4.23) from cucumber seeds was purified by ammonium sulphate fractionation, chromatography on immobilized pepstatin and gel filtration on Sephacryl S-200. The preparation obtained, homogeneous on polyacrylamide-gel electrophoresis in acidic and alkaline media, has a molecular mass of 42,000, pI of 5.2, and shows the highest activity with denatured haemoglobin at pH 3.2. The proteinase is stable in slightly alkaline medium, whereas it is inactivated in acidic medium, especially in the presence of NaCl. The enzyme activity is affected neither by the inhibitors of serine proteinases, sulfhydryl-proteinases and metalloproteinases, nor by divalent metal ions, whereas the enzyme is inactivated by the inhibitors of aspartyl proteinases: 1,2,3-epoxy(p-nitrophenoxy)propane, diazoacetyl-DL-norleucine and pepstatin.
D016282:Aspartic Acid Endopeptidases; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism*; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010436:Pepstatins / Q000302:isolation & purification; D011480:Protease Inhibitors; D012639:Seeds / Q000201:enzymology*; D012965:Sodium Chloride / Q000494:pharmacology; D013696:Temperature; D014362:Trypsinogen / Q000378:metabolism
D010436:Pepstatins; D011480:Protease Inhibitors; C014195:Streptomyces pepsin inhibitor; D012965:Sodium Chloride; D014362:Trypsinogen; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; C031375:pepstatin