Lectins are proteins or glycoproteins, originally isolated from plant seeds. Characteristics are their ability to bind glycoproteins or glycolipids depending on the carbohydrate residues. The present review describes the structure of the lectins, their binding specificity and their functions with respect to precipitation of glycoproteins, agglutination of cells, transformation of lymphocytes and toxic action. Recently, lectin-analogs have been described in rabbit liver, which are responsible for hepatic uptake of circulating glycoproteins. The regulation of this process is intimately linked to the terminal N-Acetylneuraminic acid (NA-NA). Moreover, its significance is shown during fetal development, oncogenic transformation, immunologic recognition as well as homostasis. Due to the different terminal carbohydrate residues, glycoproteins of adult, fetal or transformed cells can be separated using affinity chromatography. Besides the purification of glycoproteins, lectins are also used for the separation of intact cells. Therefore the use of lectins is recommended for preparative and analytical methods, for the measurements of glycoprotein-turnover and for clinical diagnostics.