Modifications in the purification protocol of Celosia cristata antiviral proteins lead to protein that can be N-terminally sequenced.
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.
Gholizadeh
Ashraf
A
Division of Biochemistry, Indian Agricultural Research Institute, New Delhi-12, India.
Kapoor
H C
HC
D000595:Amino Acid Sequence; D000998:Antiviral Agents / Q000235:genetics / Q000302:isolation & purification* / Q000494:pharmacology; D001681:Biological Assay; D034762:Celosia / Q000235:genetics* / Q000821:virology; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D010940:Plant Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000494:pharmacology; D010942:Plant Viruses / Q000187:drug effects; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein
D000998:Antiviral Agents; D010940:Plant Proteins