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Cytotoxic effects of lectins.
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The interaction of lectins with various normal or malignant cells not infrequently results in their proliferation or death (1-3). Incubation of normal T-lymphocytes with some lectins, such as Con A and PHA stimulates their proliferation and renders them highly cytotoxic and capable of lysing various
Binding properties of a blood group Le(a+) active sialoglycoprotein, purified from human ovarian cyst, with applied lectins.
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Studies on the structures and binding properties of the glycoproteins, purified from human ovarian cyst fluids, will aid the understanding of the carbohydrate alterations occurring during the biosynthesis of blood group antigens and neoplasm formation. These glycoproteins can also serve as important
Influence of Concanavalin A, wheat germ agglutinin, and soybean agglutinin on the fusion of myoblasts in vitro.
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Although muscle cell fusion was shown to be an energy-requiring process, release of myoblasts from an EGTA fusion block could be accomplished with Earle's balanced salt solution (containing 1.8 mM Ca++) free of glucose or any other energy-produced metabolite. The effect of concanavalin A, abrin, and
Recognition roles of the carbohydrate glycotopes of human and bovine lactoferrins in lectin-N-glycan interactions.
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BACKGROUND
Lactoferrin is an iron-binding protein belonging to the transferrin family. In addition to iron homeostasis, lactoferrin is also thought to have anti-microbial, anti-inflammatory, and anticancer activities. Previous studies showed that all lactoferrins are glycosylated in the human body,
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