Modifications in the Purification Protocol of Celosia Cristata Antiviral Proteins Lead to Protein that Can Be N-Terminally Sequenced
Abstract:Plants antiviral proteins are being used as anticancer agents and inhibit other viral diseases in humans. We modified the purification protocol of the two N-terminally blocked antiviral glycoproteins, CCP-25 and CCP-27, purified from the leaves of Celosia cristata. This not only gave rise to single pure samples with few steps of purification but also resulted in N-terminally free proteins. The extra purity of the samples was analyzed by reverse phase HPLC. Deglycosylation studies of CCP-25 with PNGase F enzyme revealed that its asparagine or asparagine-linked glycon contents are negligible. Partial N-terminal sequence of the CCP-25 showed the sequence (ANDIS), which seems to be conserved among plant antiviral proteins.
Document Type: Review Article
Affiliations: Division of Biochemistry, Indian Agricultural Research Institute, New Delhi-12, India.
Publication date: December 1, 2004
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