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Immunochemical behavior of a plant agglutinin (lectin)

Archives of Biochemistry and Biophysics, 1955
Abstract Methods of purification of the A-specific hemagglutinin (lectin) from lima beans are presented, and the results of ultracentrifugal and electrophoretic determinations on the partially purified protein. Preparations were obtained in which over 30% of the protein was specifically precipitable by A substance.
W C, BOYD, E, SHAPLEIGH, M, McMASTER
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History of Plant Lectin Research

2014
Numerous plant species are known to express one or more lectins or proteins containing a lectin domain, enabling these proteins to select and bind specific carbohydrate structures. The group of plant lectins is quite heterogeneous since lectins differ in their molecular structure, specificity for certain carbohydrate structures, and biological ...
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Fractionation of human lymphocytes with plant lectins

Cellular Immunology, 1979
Abstract We have fractionated human peripheral blood lymphocytes (PBL) into distinct subclasses based upon differential adherence to the plant lectins wheat germ agglutinin (WGA) and Lens culinaris lectin (lentil-PHA), derivatized to gelatin surfaces in plastic tubes and Petri dishes.
David H Boldt, Ruth D Lyons
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Uses of plant lectins in bioscience and biomedicine

Frontiers in Bioscience, 2008
New research directions in the last decade have led to major developments in the uses of plant lectins in bioscience and biomedicine. Major advances have been made in our understanding how lectins in the diet can act on the gastrointestinal tract and the physiological consequences of their actions, and how they can modulate body- and organ metabolism ...
Arpad, Pusztai   +2 more
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Inhibition of interferon action by plant lectins

Nature, 1974
IN spite of various theories, the mechanism of the antiviral action of interferon1–3 remains obscure. Previous work indicated that it does not have to penetrate into target cells to exert its effect. Mouse interferon preparations, when covalently bound to Sepharose beads, retained full antiviral activity, even after multiple cell-to-cell transfers4 ...
F, Besancon, H, Ankel
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Carbohydrate-Binding Sites of Plant Lectins

1988
Lectins are a diverse group of proteins and glycoproteins that exhibit specific binding for certain carbohydrates. Proteins with this property have been described in a wide variety of taxa, ranging from bacteria (e.g. Neter 1956) to slime molds (Barondes and Haywood 1979) and lower vertebrates (Simpson et al.
G N, Reeke, J W, Becker
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Principles of structures of animal and plant lectins

Biochimica et Biophysica Acta (BBA) - General Subjects, 2002
Lectins form a diverse group of protein families that have in common their ability to specifically recognize certain carbohydrates. Crystal structures of members of the different animal and plant lectin families have revealed a wide variety of lectin folds and carbohydrate binding site architectures.
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Isolation of Plant Lectins

1993
Lectins are carbohydrate-binding proteins of nonimmune origin which occur throughout the biosphere (Goldstein and Poretz 1986). Their most obvious property, hemagglutination, has been known for more than a century (Franz 1988), whereas the art of purifying lectins is much younger.
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Plant Lectins

2021
Abdullah Bin Abdul Nazar   +3 more
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Plant Lectins (Phytohemagglutinins)

1976
It was already recognized at the end of the last century that proteins in extracts of certain plants are able to agglutinate red blood cells. For a long time this potency has been regarded as a curiosity only. Retrospectively however, it can be said that studies with the respective proteins were landmarks in the elucitation of the basic mechanisms of ...
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