, Volume 119, Issue 1, pp 39–46 | Cite as

Digestive enzymes secreted by the carnivorous plant Nepenthes macferlanei L.

  • Zoltán A. Tökés
  • Wang Chee Woon
  • Susan M. Chambers


At least two proteases are present in the secretion of the pitchers of Nepenthes macferlanei, a major one with an estimated molecular weight of 59000 and a minor one of 21000. The specificity of the major enzyme, nepenthesin, was broader than previously reported, and strikingly similar to that of pepsin. Lipase activity was also demonstrated, while no amylase activity was present.


Enzyme Molecular Weight Lipase Amylase Digestive Enzyme 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Amagase, S., Nakayama, S., Tsugita, A.: Acid protease in Nepenthes. II. Study on the specificity of nepenthesin. J. Biochem. 66, 431–439 (1969)Google Scholar
  2. Bayliss, R. S., Knowles, J. R., Wybrandt, G. B.: An aspartic acid residue at the active site of pepsin. Biochem. J. 113, 377–386 (1969)Google Scholar
  3. Gray, W. R., Dansyl chloride procedure. In: Methods in enzymology, vol. XI, p. 139–151, Hirs, C. H. W., ed. New York-London: Acad. Press 1967Google Scholar
  4. Jentsch, J.: Probleme bei der Reinigung von Nepenthes-Kannensansaft-Enzymen. Ber. dtsch. bot. Ges. 83, 171–176 (1970)Google Scholar
  5. Johnson, M. J.: Isolation and Properties of a pure yeast polypeptidase. J. boil. Chem. 137, 575–586 (1941)Google Scholar
  6. Katz, A. M., Dreyer, W. J., Anfinsen, C. B.: Peptide separation by two-dimensional chromatography and electrophoresis. J. biol. Chem. 234, 2897–2900 (1959)Google Scholar
  7. Lüttge, U.: Drüsenfunktionen bei fleischfressenden Pflanzen. Umsch. Wiss. Techn. 67, 181–186 (1967)Google Scholar
  8. Mangold, H. K.: Aliphatic lipids. In: Thin-layer chromatography, p. 375–394, Stahl, E., ed. Berlin-Heidelberg-New York: Springer 1969Google Scholar
  9. Margoliash, E., Smith, E. L., Kreil, G., Tuppy, H.: Amino acid sequence of horse heart cytochrome c: The complete amino acid sequence. Nature (Lond.) 192, 1125–1127 (1961)Google Scholar
  10. Mathews, R. E. F.: A ribonuclease from Nepenthes spp. Biochim. biophys. Acta (Amst.) 28, 552–553 (1960)Google Scholar
  11. Moore, S., Stein, W. H.: A modified ninhydrin reagent for the photometric determination of amino acids and related compounds. J. biol. Chem. 211, 907–913 (1954)Google Scholar
  12. Morishima, H., Takita, T., Aoyagi, T., Takeuchi, T., Umezawa, H.: The structure of pepstatin. J Antibiot. (Tokyo), Ser. A 23, 263–265 (1970)Google Scholar
  13. Nakayama, S., Amagase, S.: Acid protease in Nepenthes: partial purification and properties of the enzyme. Proc. Japan Acad 44, 358–362 (1968)Google Scholar
  14. Potty, V. H.: Determination of proteins in the presence of phenols and pectins. Analyt. Biochem. 28, 535–539 (1969)Google Scholar
  15. Somogyi, M.: Notes on sugar determination. J. biol. Chem. 195, 19–23 (1952)Google Scholar
  16. Steckelberg, R., Lüttge, U., Weigl, J.: Reinigung der Proteinase aus Nepenthes-Kannensaft. Planta (Berl.) 76, 238–241 (1967)Google Scholar

Copyright information

© Springer-Verlag 1974

Authors and Affiliations

  • Zoltán A. Tökés
    • 1
  • Wang Chee Woon
    • 2
  • Susan M. Chambers
    • 3
  1. 1.Department of BiochemistryUniversity of MalayaKuala LumpurMalaysia
  2. 2.Division of BotanyUniversity of MalayaKuala LumpurMalaysia
  3. 3.Basel Institute for ImmunologyBaselSwitzerland

Personalised recommendations