Changes

[[File:Mistletoe Lectin.jpg|thumb|308x308px|Viscum album agglutinin (VAA-I) consists of two chains. The A-chain (white) with a molecular weight of 29 kDa and with N-glycosidase activity is a potent ribosomal inactivator. The sugar-binding B-chain (green) with a molecular weight of 34 kDa is responsible for the immunomodulatory effect of the molecule. Red colored parts of the B-chain indicate the sugar-binding receptors. (The picture was kindly provided by Madaus Ag, Germany.) Hajtó, T., Hostanska, K., Berki, T., Pálinkás, L., Boldizsár, F., & Németh, P. (2005). Oncopharmacological perspectives of a plant lectin (Viscum album agglutinin-I): overview of recent results from in vitro experiments and in vivo animal models, and their possible relevance for clinical applications. Evidence-Based Complementary and Alternative Medicine, 2(1), 59–67. Published by Oxford University Press.]]

[[File:Mistletoe Lectin.jpg|thumb|308x308px|Viscum album agglutinin (VAA-I) consists of two chains. The A-chain (white) with a molecular weight of 29 kDa and with N-glycosidase activity is a potent ribosomal inactivator. The sugar-binding B-chain (green) with a molecular weight of 34 kDa is responsible for the immunomodulatory effect of the molecule. Red colored parts of the B-chain indicate the sugar-binding receptors. (The picture was kindly provided by Madaus Ag, Germany.) Hajtó, T., Hostanska, K., Berki, T., Pálinkás, L., Boldizsár, F., & Németh, P. (2005). Oncopharmacological perspectives of a plant lectin (Viscum album agglutinin-I): overview of recent results from in vitro experiments and in vivo animal models, and their possible relevance for clinical applications. Evidence-Based Complementary and Alternative Medicine, 2(1), 59–67. Published by Oxford University Press.]]

==== Structure of Mistletoe Lectins ====

====Structure of Mistletoe Lectins====

Viscum album contains three lectins, differing in their specificity for glycoprotein sites on cell membranes. These are mistletoe lectin 1, 2, and 3 or ML-1, Ml-2, and ML-3. Mistletoe lectin 1 has had the most amount of research. Mistletoe lectins, as members of the type 2 RIP family, are composed of two protein portions linked by a disulfide bond. The A chain is a strong inhibitor of the ribosome, the cellular protein manufacturing organelle. The B chain has strong and selective binding affinity to carbohydrate molecules on the cell surface.<ref>{{cite journal | vauthors=((Hajtó, T.)), ((Hostanska, K.)), ((Berki, T.)), ((Pálinkás, L.)), ((Boldizsár, F.)), ((Németh, P.)) | journal=Evidence-Based Complementary and Alternative Medicine | title=Oncopharmacological perspectives of a plant lectin (Viscum album agglutinin-I): overview of recent results from in vitro experiments and in vivo animal models, and their possible relevance for clinical applications | volume=2 | issue=1 | pages=59–67 | date= 2005}}</ref>

Viscum album contains three lectins, differing in their specificity for glycoprotein sites on cell membranes. These are mistletoe lectin 1, 2, and 3 or ML-1, Ml-2, and ML-3. Mistletoe lectin 1 has had the most amount of research. Mistletoe lectins, as members of the type 2 RIP family, are composed of two protein portions linked by a disulfide bond. The A chain is a strong inhibitor of the ribosome, the cellular protein manufacturing organelle. The B chain has strong and selective binding affinity to carbohydrate molecules on the cell surface.<ref>{{cite journal | vauthors=((Hajtó, T.)), ((Hostanska, K.)), ((Berki, T.)), ((Pálinkás, L.)), ((Boldizsár, F.)), ((Németh, P.)) | journal=Evidence-Based Complementary and Alternative Medicine | title=Oncopharmacological perspectives of a plant lectin (Viscum album agglutinin-I): overview of recent results from in vitro experiments and in vivo animal models, and their possible relevance for clinical applications | volume=2 | issue=1 | pages=59–67 | date= 2005}}</ref>

 

==Scientific Evidence==

==Scientific Evidence==