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Isolation and characterization of two Korean mistletoe lectins.
- Source :
-
Journal of biochemistry and molecular biology [J Biochem Mol Biol] 2007 Nov 30; Vol. 40 (6), pp. 959-65. - Publication Year :
- 2007
-
Abstract
- Two isolectins (KML-IIU and the KML-IIL) were individually isolated from the previously reported Korean mistletoe lectin, KML-C, by using an immunoaffinity column. Molecular weights of the KML-IIU and the KML-IIL were 64 kDa and 60 kDa respectively. Both of the lectins were composed of heterogeneous A and B subunits linked with a disulfide bond, and showed the same carbohydrate-binding specificities for Gal and GalNAc. However, they are different not only in biophysical properties (glycosylation and amino acid compositions) but also bioactivities (cell killing and cytokine induction). The KML-IIL showed 17-145 times stronger in cytotoxicities to various human and mouse cancer cell lines than the KML-IIU. The KML-IIL also induced TNF-alpha secretion from mouse peritoneal macrophages 4.5 times better than the KML-IIU. The results demonstrated isolectins in Korean mistletoe were varied in bioactivities and the KML-IIL may be developed as an anti-cancer agent.
- Subjects :
- Amino Acids analysis
Animals
Antineoplastic Agents, Phytogenic chemistry
Antineoplastic Agents, Phytogenic isolation & purification
Antineoplastic Agents, Phytogenic pharmacology
Cell Line, Tumor
Glycosylation
Humans
In Vitro Techniques
Korea
Macrophages, Peritoneal drug effects
Macrophages, Peritoneal immunology
Mice
Mice, Inbred BALB C
Molecular Weight
Plant Preparations chemistry
Plant Preparations pharmacology
Plant Proteins chemistry
Plant Proteins pharmacology
Protein Subunits
Ribosome Inactivating Proteins chemistry
Ribosome Inactivating Proteins pharmacology
Ribosome Inactivating Proteins, Type 2
Toxins, Biological chemistry
Toxins, Biological pharmacology
Tumor Necrosis Factor-alpha biosynthesis
Mistletoe chemistry
Plant Preparations isolation & purification
Plant Proteins isolation & purification
Ribosome Inactivating Proteins isolation & purification
Toxins, Biological isolation & purification
Subjects
Details
- Language :
- English
- ISSN :
- 1225-8687
- Volume :
- 40
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Journal of biochemistry and molecular biology
- Publication Type :
- Academic Journal
- Accession number :
- 18047792
- Full Text :
- https://doi.org/10.5483/bmbrep.2007.40.6.959