| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 5168039 | Phytochemistry | 2006 | 13 Pages |
Abstract
A glycosylated serine protease from the latex of medicinal plant Euphorbia milii has been isolated, and comprehensively studied. Its activity over a broad range of pH and temperature, high stability against the chemical and physiological denaturants and less susceptibility to autodigestion makes the enzyme applicable in biotechnology industries.
Keywords
N-ethyl-maleimideβMEpCMBTFMSN-ethyl maleimideGuHClEuphorbiaceaeBAPATEMEDdiisopropylfluorophosphatePMSFDTNBDFPHEPESIAATCAEGTATFADTTβ-mercaptoethanolEDTAEuphorbia miliiTrifluoroacetic acidiodoacetic acidEnzyme-linked immunosorbent assayELISAdithiothreitolsoybean trypsin inhibitorNEMSerine proteasesGuanidine hydrochloride
Related Topics
Physical Sciences and Engineering
Chemistry
Organic Chemistry
Authors
Subhash C. Yadav, Monu Pande, M.V. Jagannadham,