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The importance of glycosylation in biological events and the role it plays in glycoprotein function and structure is an area in which there is growing interest. In order to understand how glycosylation affects the shape or function of a protein it is however important to have suitable techniques available to obtain structural information on the oligosaccharides attached to the protein. For many years the complexity of the structures required sophisticated analytical techniques only available to a few specialist laboratories. In many cases these techniques were not available or required a large amount of material and therefore the number of glycoproteins which were fully characterised were relatively few. In recent years there have been substantial developments in the analysis of glycosylation which has significantly changed the capability to fully characterise molecules of biological interest. A number of different techniques are available which differ in terms of their complexity, the amount of information which is available from them, the skill needed to perform them and their cost. It is now possible for many laboratories who do not specialise in glycosylation analysis to obtain some information although this may be incomplete. These developments do, however, also make complete characterisation of a glycoprotein a much less daunting task and in many cases this can be performed more easily and with less starting material than was previously required. In this review a summary will be given of current techniques and their suitability for different types of analysis will be considered.
There is observed increasing pollution of environment by nitrosocompounds. Acute intoxication of animals by nitrosocompounds lead to necrosis and chronic exposure to neoplasm. We have little information on the influence of nitrosocompounds on metabolism of glycoconjugates (glycoproteins, glycolipids and proteoglycans) in animals. The aim of our work is evaluation the influence of exposure of rats for 10 and 90 days to N-nitrosodimethylamine (NDMA), on activity of lysosomal exoglycosidases (enzymes hydrolysing terminal sugars in oligosaccharides) in the alimentary tract. It was found that intoxication of rats with NDMA increased specific activity of N-acetyl-b-hexosaminidase, b-galactosidase and a-mannosidase in majority of tissues of rat alimentary tract. Damage the cells of alimentary tract by NDMA or its metabolites, increase activity of exoglycosidases, because damaged tissue elements must be removed by catabolic enzymes before restoration processes can start.
Work in cadmium (Cd) smelter and smoking cigarettes damages teeth and oral mucosa which are protected by tissue and salivary glycoconjugates: glycoproteins, glycolipids, and proteoglycans. We worked out a rat model imitating human "envi­ronmental" and "occupational" exposure to cadmium using 5 mg Cd and 50 mg Cd/l in drinking water, respectively. In submandibulary glands of exposed to Cd rats, we found the time and dose dependent accumulation of Cd and simultanous decrease in activity of ß-N-acetylhexosaminidase (HEX). In homogenates of submandibulary glands of control rats, ß-N-acetylhexosa- minidase showed the highest activity. The activities of a-mannosidase and ß-galacto- sidase were very low. None of these exoglycosidases were inhibited by Cd even at 44 mM concentration.
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