A Novel Serine Protease Cryptolepain from Cryptolepis buchanani: Purification and Biochemical Characterization
A Novel Serine Protease Cryptolepain from Cryptolepis buchanani: Purification and Biochemical Characterization
- J. Agric. Food Chem., 54(26), p.10141-10150, 2006 .
A novel protease is purified to homogeneity from the latex of a medicinally important plant Cryptolepis buchanani of family Apocynaceae (formerly Asclepiadaceae). The enzyme named cryptolepain has a molecular mass of 50.5 kDa. The isoelectric point and extinction coefficient (¤280nm 1
ASCLEPIDACEAE
APOCYNACEAE
SERINE PROTEASES
PLANT ENDOPEPTIDASE
CRYPTOLEPIS BUCHANANI
CRYPTOLEPAIN
ANTI-CRYPTOLEPAIN
A novel protease is purified to homogeneity from the latex of a medicinally important plant Cryptolepis buchanani of family Apocynaceae (formerly Asclepiadaceae). The enzyme named cryptolepain has a molecular mass of 50.5 kDa. The isoelectric point and extinction coefficient (¤280nm 1
ASCLEPIDACEAE
APOCYNACEAE
SERINE PROTEASES
PLANT ENDOPEPTIDASE
CRYPTOLEPIS BUCHANANI
CRYPTOLEPAIN
ANTI-CRYPTOLEPAIN
