RRC ID 49565
Author Narita H, Asaka Y, Ikura K, Matsumoto S, Sasaki R.
Title Isolation, characterization and expression of cationic peroxidase isozymes released into the medium of cultured tobacco cells.
Journal Eur J Biochem
Abstract Three glycoproteins of 34, 38 and 40 kDa were isolated from the spent medium of suspension-cultured tobacco cells. The 38-kDa and 40-kDa proteins were highly cationic peroxidases with indistinguishable enzymic properties but their structural difference was confirmed by sequence analysis of the amino-terminal regions and the recognition specificity of monoclonal antibodies. The 34-kDa protein was a moderately cationic peroxidase with enzymic properties quite different from those of the 38-kDa and 40-kDa enzymes. They were undetectable in the spent medium during the cell-proliferation phase but became abundant in the medium during the cell-expansion phase. This was confirmed quantitatively with the 40-kDa protein using the 40-kDa-specific monoclonal antibody. The mRNA expression for 40-kDa protein was at a constant basal level in the cell-proliferation phase but increased in the cell-expansion phase.
Volume 228(3)
Pages 855-62
Published 1995-3-15
PMID 7737186
MeSH Amino Acid Sequence Animals Antibodies, Monoclonal / immunology Blotting, Northern Cells, Cultured Culture Media Enzyme-Linked Immunosorbent Assay Female Isoenzymes / genetics Isoenzymes / immunology Isoenzymes / isolation & purification* Isoenzymes / metabolism Mice Mice, Inbred BALB C Molecular Sequence Data Peroxidases / genetics Peroxidases / immunology Peroxidases / isolation & purification* Peroxidases / metabolism Plant Proteins / isolation & purification Plant Proteins / metabolism Plants, Toxic* Tobacco / enzymology*
Times Cited 23
DNA material pC (RDB01851) pD (RDB01852).