Modifications in the Purification Protocol of Celosia Cristata Antiviral Proteins Lead to Protein that Can Be N-Terminally Sequenced
- 1 December 2004
- journal article
- Published by Bentham Science Publishers Ltd. in Protein & Peptide Letters
- Vol. 11 (6) , 555-561
- https://doi.org/10.2174/0929866043406210
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.Keywords
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