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Titlebook: Lectins; N. Sharon,H. Lis Book 1989 Nathan Sharon and Halina Lis 1989 biosynthesis.carbohydrate.enzyme.enzymes.immunoglobulin.macromolecul

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Molecular properties, of them, except that they are proteins and that they consist of subunits or protomers. Their molecular weights range from 8500 Da (the lectin from stinging nettle stems) to 400 000 Da (. lectin). Some lectins are very unusual in their composition and structure. Striking examples are the lectins fro
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Three dimensional structures,mensional structure of the protein, which is best obtained by X-ray crystallography. Many lectins are now being investigated by this method. The structures at high resolution of three legume lectins (concanavalin A, pea lectin and favin), of one cereal lectin (wheat germ agglutinin) and of ricin hav
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Biosynthesis,ssue slices and cell free systems, as well as the application of recombinant DNA techniques. As with most proteins, the information for lectin synthesis, encoded in the genes and transmitted by mRNA, is utilized by the ribosomes to form precursor polypeptides in the endoplasmic reticulum. These prec
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Functions in nature,provided a major stimulus for the continuing search for their physiological function(s). A strong argument that lectins indeed have such functions is the fact that they have been conserved throughout evolution as homologous families of proteins. Another argument is that many of them are developmenta
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al, accessible material that will appeal to academics and pr.This book provides an in-depth view of supplier diversity programs and how they have contributed to the meteoric rise of minority businesses. Incorporating expert advice from supplier diversity practitioners as well as empirical data, it l
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N. Sharon,H. Lisal, accessible material that will appeal to academics and pr.This book provides an in-depth view of supplier diversity programs and how they have contributed to the meteoric rise of minority businesses. Incorporating expert advice from supplier diversity practitioners as well as empirical data, it l
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