Modifications in the Purification Protocol of Celosia Cristata Antiviral Proteins Lead to Protein that Can Be N-Terminally Sequenced
Authors: Gholizadeh, Ashraf; Kapoor, H. C.
Source: Protein and Peptide Letters, Volume 11, Number 6, December 2004 , pp. 555-561(7)
Publisher: Bentham Science Publishers
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
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.