By Leonard Warren
Sure carbohydrates are an enormous and engaging subject in biochemical and melanoma learn. in accordance with a chain of invited lectures, this e-book makes a speciality of the targeted function that certain carbohydrates play in nature and replicate the author's special profession in biochemical study. another subject matters coated are the houses of membrane glycoproteins, fascinated about the resistance of cells to medicines, and the metabolism of sugars and sialic acids, either one of which shape a pivotal position within the author's stories. The publication chronicles just a few of the large advances which have been made in biochemistry over the last few a long time.
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Additional info for Bound carbohydrates in nature
The levels of sialyl transferases may be of special significance in glycoprotein Cambridge Books Online © Cambridge University Press, 2010 Cambridge Books Online © Cambridge University Press, 2012 40 (i) Derivatives of neuraminic acid biosynthesis because, when a sialic acid is added, no further chain elongation occurs: the sialic acid is a 'capper' or chain terminator. Thus, the level of sialyl transferase(s) may determine the size of the bound sugar groups. In general, every intermediate structure formed may be competed for by more than one enzyme.
It is apparent from the data of Fig. 1 that the glycopeptides derived from chondroblasts rapidly growing in suspension or in monolayer are considerably larger than those from chondroblasts in situ, in organ culture, or in a compact pellet. The larger glycopeptides elute earlier (a, b9 c). Similarly, when hamster cells are grown in culture on glass, plastic or plastic coated with collagen, the populations of bound carbohydrate are clearly different (Warren, Blithe and Cossu, 1982). The differences could be explained by differential productions of specific glycoproteins, each with its own complement of carbohydrate groups.
Finally, UDP-Nacetylglucosamine can undergo a complex and irreversible epimerization at C-2, accompanied by hydrolysis at C-l, to form Af-acetylmannosamine and UDP (Reaction 12). The labile enzyme that catalyzes the reaction requires no coenzymes or factors. H2O UDP-Af-acetylglucosamine -> A^-acetylmannosamine + UDP (12) N-Acetylmannosamine can also be formed directly from 7V-acetylglucosamine (Ghosh and Roseman, 1965 a) (Reaction 13). Af-acetylglucosamine < > N-acetylmannosamine (13) It is possible that the function of the enzyme catalyzing this reaction is to rid the cell of excess N-acetylmannosamine and thus regulate the level of sialic acid biosynthesis.