Proteolytic activity in latex of the genus Euphorbia--a chemotaxonomic marker?
Eighteen species of the genus Euphorbia are known to have proteolytic enzymes in their latices, 9 of them are characterized by the type of endopeptidases (Cysteine-, Serine-, Metallo- or Aspartatic-endopeptidase) which are responsible for the activity, and all nine are serine endopeptidases. In our study we examined the latices of 64 different species of the genus Euphorbia concerning proteolytic activity and serine protease activity, five of them are mentioned in the literature to be proteolytic active and four are known to contain at least one serine endopeptidase. All tested samples were able to degrade labelled casein, the activity of six latices were completely inhibited by specific serine protease inhibitors, 15 samples were not influenced, and in 43 latices a remaining activity was measured, indicating that other types of endopeptidases seem to be involved.
Domsalla
A
A
Institute of Pharmacy, Free University Berlin, Berlin, Germany.
Görick
C
C
Melzig
M F
MF
D015415:Biomarkers; D002364:Caseins / Q000737:chemistry; D002965:Classification / Q000379:methods; D010450:Endopeptidases / Q000737:chemistry*; D028481:Euphorbia / Q000145:classification* / Q000201:enzymology*; D007202:Indicators and Reagents; D007840:Latex / Q000032:analysis*; D011480:Protease Inhibitors / Q000494:pharmacology; D057057:Serine Proteases / Q000032:analysis / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology
D015415:Biomarkers; D002364:Caseins; D007202:Indicators and Reagents; D007840:Latex; D011480:Protease Inhibitors; D015842:Serine Proteinase Inhibitors; D010450:Endopeptidases; D057057:Serine Proteases