The lectin fromViscum album L. purification by biospecific affinity chromatography

Ziska, P; Franz, Hartmut; Kindt, A

doi:10.1007/bf01921941

Cited by 52 publications

(13 citation statements)

References 5 publications

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“…The authors suggest that this was due to the presence of viscotoxins. Ziska et al (1978) isolated 0.4 mg ML I perg fresh plant. In our experiments only about 1/ 300000 of this amount would be sufficient to be in the range of the EDso of Molt4 cells (EDso= 1.3 ng/mL).…”

Section: Discussionmentioning

confidence: 99%

Comparative study on the cytotoxic effect of viscotoxin and mistletoe lectin on tumour cells in culture

Urech

Schäller

Ziska³

et al. 1995

Phytotherapy Research

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A comparative study was carried out on the effect of viscotoxin and mistletoe lectin I, two mistletoe proteins known to be toxic to mammals, on three tumour cell lines in culture (Yoshida sarcoma cells, T-cell leukaemia cells Molt4, and myeloid cells K562). Both viscotoxin and mistletoe lectin were cytotoxic for the three cell lines tested, although the cell sensitivity was dependent on the type of cells used. Yoshida cells were the most sensitive to viscotoxin (EDSo=0.7 pg/mL) and less sensitive to mistletoe lectin (EDSo= 12.8 pg/mL). K562 cells were more sensitive to mistletoe lectin (EDSo=75 pg/mL) than Molt4 cells (EDSo= 1.3 ng/mL), whose high sensitivity to mistletoe lectin is well known. Data are also reported showing that this cell line dependent sensitivity can be exploited to demonstrate and/or to discriminate the toxic activities of either substances in crude mistletoe extracts. In particular the Yoshida cell line can represent a suitable system for a bioassay of viscotoxin in these extracts.

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Section: Discussionmentioning

confidence: 99%

Comparative study on the cytotoxic effect of viscotoxin and mistletoe lectin on tumour cells in culture

Urech

Schäller

Ziska³

et al. 1995

Phytotherapy Research

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“…Lectin I (MLI) from Viscum album was prepared in the Staatliches Institut für Immunpräparate und Nährmedien, Berlin, FRG, according to the method described by Ziska et al [26]. The MLI preparation (charge no.…”

Section: Methodsmentioning

confidence: 99%

Induction of tumor necrosis factor expression by a lectin fromViscum album

Männel

Becker

Gundt

et al. 1991

Cancer Immunol Immunother

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A purified lectin (MLI) from Viscum album was used to test whether peripheral monocytes from human blood can be activated for the production of tumour necrosis factor (TNF). Cytotoxic activity was detected in the supernatant of MLI-stimulated monocyte cultures. This cytotoxic activity was completely inhibited by monoclonal antibodies to TNF alpha. Small amounts of soluble TNF protein were measured in a TNF alpha-specific enzyme-linked immunospecific assay system. Strong expression of TNF alpha mRNA was induced in human monocytes as well as in macrophage cultures from C3H/HeJ mice having a low response to endotoxin after 2 h of stimulation. Both chains of the MLI were found to induce TNF mRNA equally well in human monocytes. In macrophages of endotoxin-low-responder mice the toxic A chain was a better inducer of TNF mRNA than the galactose-specific lectin B chain. Thus, MLI has immunomodulating effects in activating monocytes/macrophages for inflammatory responses.

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“…The supernatant was purified by filtration (Sterivex GV Filter, Millipore) and adjusted to 100 ml with peptide eluent (0.05 M K2HP04*3HzO in 0.15 M NaCI, pH 7.0). The solution was applied to an affinity chromatography column on divinyl sulfone-activated lactose-coupled Sepharose 4B (3 X 50 cm) to isolate ML-I from the mistletoe extract [15]. The column had previously been equilibrated and was then eluted with the same buffer.…”

Section: Protein Isolationmentioning

confidence: 99%

Complete amino acid sequence of the A chain of mistletoe lectin I

Soler

Stoeva

Schwamborn³

et al. 1996

FEBS Letters

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The complete amino acid sequence of the A chain of mistletoe lectin I was determined via Edman degradation sequencing of the N-terminus and tryptic and endoproteinase Asp-N overlapping fragments, amino acid analysis and MALDI-MS. The data obtained show a great homology with the chains of ribosome-inactivating proteins such as ricin and abrin with 111 (abrin-a) and 103 (ricin-D) amino acid residues conserved, respectively. The knowledge of the primary structure of MLA will have a fundamental impact on elucidating the biological function of medically applied mistletoe lectins on a molecular basis.

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The lectin fromViscum album L. purification by biospecific affinity chromatography

Abstract: A lectin from Viscum album which specifically binds to D-galactose was isolated by affinity chromatography on O-lactosyl-, O-galactosyl-polycarylamide or hydrolized sepharose 4 B. Some serological and physicochemical properties of the agglutination are reported.

Cited by 52 publications

References 5 publications

Comparative study on the cytotoxic effect of viscotoxin and mistletoe lectin on tumour cells in culture

Comparative study on the cytotoxic effect of viscotoxin and mistletoe lectin on tumour cells in culture

Induction of tumor necrosis factor expression by a lectin fromViscum album

Complete amino acid sequence of the A chain of mistletoe lectin I

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