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A Novel Serine Protease Cryptolepain from Cryptolepis buchanani: Purification and Biochemical Characterization

Tipo de material: TextoTextoSeries ; J. Agric. Food Chem., 54(26), p.10141-10150, 2006Trabajos contenidos:
  • Pande, M
  • Dubey, V.K
  • Yadav, S.C
  • Jagannadham, M.V
Tema(s): Recursos en línea: Resumen: 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
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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

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