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Animal lectins Gabius HJEur J Biochem 1997[Feb]; 243 (3): 543-76Protein and lipid glycosylation is no longer considered as a topic whose appeal is restricted to a limited number of analytical experts perseveringly pursuing the comprehensive cataloguing of structural variants. It is in fact arousing curiosity in various areas of basic and applied bioscience. Well founded by the conspicuous coding potential of the sugar part of cellular glycoconjugates which surpasses the storage capacity of oligonucleotide- or oligopeptide-based code systems, recognition of distinct oligosaccharide ligands by endogenous receptors, i.e. lectins and sugar-binding enzymes or antibodies, is increasingly being discovered to play salient roles in animal physiology. Having inevitably started with a descriptive stage, research on animal lectins has now undubitably reached maturity. Besides listing the current categories for lectin classification and providing presentations of the individual families and their presently delineated physiological significance, this review places special emphasis on tracing common structural and functional themes which appear to reverberate in nominally separated lectin and animal categories as well as lines of research which may come to fruition for medical sciences.|*Carbohydrate Metabolism[MESH]|Animals[MESH]|Carrier Proteins/*chemistry[MESH]|Humans[MESH]|Lectins/*chemistry/classification[MESH]|Receptors, Cell Surface/*chemistry[MESH] |
