Changes in T-Lymphocyte Glycoprotein Structures Associated with Differentiation
The problem to be discussed in this chapter is whether changes in the structure of lymphocyte surface glycoproteins—particularly changes in their carbohydrate portions—occur during normal lymphoid differentiation. A positive answer would argue against suggestions (reviewed in Gahmberg, 1981) that the principal role for glycoprotein carbohydrate is a general one, such as stabilizing protein structure, protecting polypeptide chains from proteolysis, or allowing transport of membrane glycoproteins to the cell surface. Information bearing on the problem is available for only a handful of proteins, of which three are major glycoprotein constituents of rodent thymocyte membranes. I will first discuss the identification and properties of these three proteins and then deal with the addition of sialic acid to these and other glycoproteins during T-lymphocyte differentiation; finally, these results will be compared to those obtained by workers studying glycoproteins from erythrocytes (the only other eukaryotic cell type for which comparable information on developmental changes in glycoprotein structure is available).
KeywordsSialic Acid Apparent Molecular Weight Sialic Acid Residue Helix Pomatia Sialic Acid Content
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