A 24,118 Da (MALDI-TOF) cysteine peptidase (EC 3.4.22.16) was purified from the latex extract of Cryptostegia grandiflora by two chromatographic steps involving ion exchange and Reverse-phase HPLC. The purified protein (Cg24-I) exhibits a single band profile following reduced SDS-PAGE and a unique
Latex proteins have drawn attention because they have shown several pharmacological activities. Herein, the fibrin(ogen)olytic activity of Cryptostegia grandiflora (CgLP) and Plumeria rubra (PrLP) latices were evaluated and characterized. Ion-exchange chromatography separated CgLP in proteolytic
It has been shown previously that the laticifer fluid of Calotropis procera (Ait.) R.Br. is highly toxic to the egg hatching and larval development of Aedes aegypti L. In the present study, the larvicidal potential of other laticifer fluids obtained from Cryptostegia grandiflora R.Br., Plumeria
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