A protease, which we designate Eumiliin, was isolated from the latex of Euphorbia milii var.
hislopii by a combination of ion-exchange chromatographic steps using DEAE-Sephacel
and gel-filtration with Sephadex G-75. Eumiliin is a monomeric protein with an apparent
molecular mass of 30kDa by SDS–PAGE under reducing conditions and gave one main
peak at 29,814 KDa in MALDI-TOF/TOF mass spectrometry. Eumiliin has caseinolytic and
fibrinogenolytic activities, but no hemorrhagic or defibrinating activities. The enzyme readily …