Comparison of Two Cysteine Endopeptidases from Latices of Morrenia brachystephana Griseb. and Morrenia odorata (Hook et Arn.) Lindley (Asclepiadaceae)

Abstract

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.