Modifications in the Purification Protocol of Celosia Cristata Antiviral Proteins Lead to Protein that Can Be N-Terminally Sequenced

Title: Modifications in the Purification Protocol of Celosia Cristata Antiviral Proteins Lead to Protein that Can Be N-Terminally Sequenced

Volume: 11 Issue: 6

Author(s): Ashraf Gholizadeh and H. C. Kapoor

Affiliation:

Keywords: antiviral, proteins, glycoproteins, celosia, purification

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.

Cite this article as:

Gholizadeh Ashraf and Kapoor C. H., Modifications in the Purification Protocol of Celosia Cristata Antiviral Proteins Lead to Protein that Can Be N-Terminally Sequenced, Protein & Peptide Letters 2004; 11 (6) . https://dx.doi.org/10.2174/0929866043406210