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KMID : 0380219940270030211
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Journal of Biochemistry and Molecular Biology
1994 Volume.27 No. 3 p.211 ~ p.216
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Catalytic and Immunological Comparison of Two Cationic Isoperoxidase from Korean Radish Root
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Abstract
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Abstract:
@EN A moderately migrating cationic isoperoxidase, designated C1, and a far migrating cationic isoperoxidase, designated C2, from Korean radish (Raphanus satuus L) root were purified to apparent homogeneity and partially characterized. These
isozymes
are glycoproteins having molecular weight of approximately 44,000 to 45,000 daltons, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration methods. The isoelectric point of isoperoxidases C1 and C2 are 8.6
and
9.0, respectively. Immunological studies involving Ouchterlony double diffusion experiments showed that cationic isoperoxidases C1 and C3 are immunologically identical. However, kinetic studies against several naturally occuring phenolic
compounds
indicated that moderately migrating cationic isoperosicases C1 has comparatively low Km values for scopoletin, ferulic acid, and esculetin when compared to the values of C3. Furthermore, isoperoxidase C1 shows a sigmoidal saturation curve for
scopoletin
oxidation inspite of its single subunit structure.
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