Isolation and properties of arginase from a shade plant, ginseng (Panax ginseng C.A. Meyer) roots

Phytochemistry. 2001 Dec;58(7):1015-24. doi: 10.1016/s0031-9422(01)00392-2.


Arginase (EC was purified to homogeneity from root tissues of three-year-old ginseng (Panax ginseng C.A. Meyer), shade plant, and was found to be an extraordinarily large molecule relatively stable to heat. The enzyme was decameric having a molecular mass of 352,000 Da, with an optimal temperature and pH of 60 degrees C and 9.5, respectively. Analogues of arginine could not replace it as substrate, and a cysteine residue is at or near the active site. Maximum activity was obtained with Mn(2+) and Co(2+) also activated the proteins, whereas, both agmatine and 5'-deoxy-methylthioadenosine were inhibitors. Specific activities of the enzyme in sliced ginseng roots were increased by plant hormones such as GA(3), IAA, kinetin and putrescine, whereas the activities of the purified enzyme were unaffected by putrescine. Increases in arginase activities by these plant hormones could affect metabolism of polyamine intracellularly.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agmatine / pharmacology
  • Arginase / antagonists & inhibitors
  • Arginase / chemistry
  • Arginase / isolation & purification*
  • Arginase / metabolism
  • Deoxyadenosines / pharmacology
  • Enzyme Inhibitors / pharmacology
  • Enzyme Stability
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Kinetics
  • Molecular Weight
  • Panax / enzymology*
  • Plant Roots / enzymology*
  • Substrate Specificity
  • Thionucleosides / pharmacology


  • Deoxyadenosines
  • Enzyme Inhibitors
  • Thionucleosides
  • 5'-methylthioadenosine
  • Agmatine
  • Arginase