Journal
BIOLOGICAL CHEMISTRY
Volume 382, Issue 5, Pages 879-883Publisher
WALTER DE GRUYTER GMBH
DOI: 10.1515/BC.2001.109
Keywords
latex peptidases; morrenain; protein purification; thiol peptidases
Categories
Ask authors/readers for more resources
The properties of morrenain b II, a proteinase isolated from the latex of Morrenia brachystephana, were compared with those of morrenain o II, a proteinase obtained from the latex of Morrenia odorata. Both peptidases were purified to homogeneity by acetone precipitation followed by cation exchange chromatography. The enzymes have pi values higher than 9.3 and similar molecular masses (close to 26 kDa) as determined by SDS-PAGE, They display maximum proteolytic activity within an alkaline pH range, and also exhibit esterolytic activity. The N-terminal sequences of morrenain o II and morrenain b II show a high degree of homology between each other and to other cysteine plant proteinases.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available