The lectin from viscum album L.—isolation, characterization, properties and structure

Luther, Peter; Theise, H; Chatterjee, Bishnu P.; Karduck, Dorit; Uhlenbruck, G.

doi:10.1016/0020-711x(80)90314-6

Cited by 40 publications

(17 citation statements)

References 7 publications

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“…This finding correlates with a previous report [19], which suggested the existence of different isolectins of Viscum album. A comparison of the obtained primary structures indicates that these two isoforms differ at least at 17 positions.…”

Section: Discussionsupporting

confidence: 82%

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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Section: Discussionsupporting

confidence: 82%

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

Soler

Stoeva

Schwamborn³

et al. 1996

FEBS Letters

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“…Since part of the arabinogalactan Fb is bound by immobilized Rieinus lectins, it was valid to assume that the galactose-specific mistletoe lectin I (ML I) [9] would also possess an affinity for this polysaccharide. However, precipitate formation in the agar diffusion test, as already described for the reaction of M L 1 with various galactans [10], could not be demonstrated. Interaction of Fb and ML I was nevertheless shown by a gel filtration method.…”

Section: Polysaccharides From Mistletoe 'Berries'mentioning

confidence: 90%

Structure and Properties of Polysaccharides from <i>Viscum album</i> (L.)

Jordan

Wagner²

1986

Oncology

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Polysaccharides are possibly involved in the pharmacological effects of Viscum album (mistletoe) extracts, which are used in cancer therapy. Therefore the water-soluble polysaccharides of the fresh plant and the fermented proprietary preparation Iscador® were isolated and characterized inter alia by methylation analysis, partial hydrolysis and C-13-NMR spectroscopy. The main polysaccharide of the green parts of Viscum is a highly esterified galacturonan whereas in Viscum ‘berries’ a complex arabinogalactan is predominant. Both types of these constituents were found in Iscador but with definite changes in molecular weight and structure. An interaction between the arabinogalactan and the galactose-specific lectin (ML I) in Viscum could be demonstrated. In three immunological tests (granulocyte, chemiluminescence, carbon clearance test) the polysaccharides failed to increase phagocytic activity of granulocytes and macrophages.

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“…chains. Investigations using polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE) and 2-mercaptoethanol showed that the mistletoe lectins consist of two different chains connected by disulfide bonds [17,31], How ever, not all chains of ML I monomers are bound via S-S bonds as originally assumed. In the electron mi croscopic picture after SDS treatment of ML 1 also smaller molecules are visible (molecular weight about 30.000 daltons), indicating noncovalently bound chains.…”

Section: Nomenclaturementioning

confidence: 99%

Mistletoe Lectins and Their A and B Chains

Franz¹

1986

Oncology

126

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Mistletoe lectins are of high biological activity. The mistletoe lectin I (ML I) is a naturally occurring conjugate of an enzyme (A chain) and a lectin (B chain). Its cytotoxicity is caused by inhibiting the protein synthesis on the ribosomal level. Prominent properties of the A chain are mitogenicity and inhibition of the protein synthesis in cell-free systems. The A chain is also a candidate for the construction of immunotoxins. The B chain as well as the intact lectins activate macrophages and release lymphokines from lymphocytes. They both inhibit the allergen-induced histamine release from leukocytes and the collagen-induced serotonin release from platelets. It cannot be excluded that the combination of selectively cytotoxic and immunopotentiating properties of mistletoe lectins and their chains are decisive for the therapeutic effects of mistletoe preparations.

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The lectin from viscum album L.—isolation, characterization, properties and structure

Cited by 40 publications

References 7 publications

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

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

Structure and Properties of Polysaccharides from <i>Viscum album</i> (L.)

Mistletoe Lectins and Their A and B Chains

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