Glycoproteins residues

The amino acid sequences for glycophorins A and A (see Refs. 8 and 19) are presented in Fig. 1. It may be clearly seen that residues 1-70 of these glycoproteins extend into the cell exterior. The hydrophobic portion of the glycoprotein, residues 71-92, appear to be imbedded in the phospholipid membrane, and residues 93-131 protrude into the cell cytoplasm. ... 

However, most biological cell membranes are not perfect two-dimensional molecular arrays. Most surfaces are composed of heterogeneous molecular assemblies and have stereolitical molecular roughness. In some cases, some molecular components of membranes extend their molecular residues into the extracellular phase at a considerable distance from the membrane surface (e.g., glycoprotein residues) as shown in Figure Such extensions of... 

An aq. soln. at 30° contains 33.3% a-Pyr, 38.5% P-Pyr, 15.4% a-Fur and 12.8% P-Fur. Found in polysialoglycoprotein of Salvelinus leucomaemis eggs. Only 6-deoxyhexose other than fucose found in glycoproteins. Residue present in some strains of Eubacterium saburreum. 

Thyroid Hormones. Iodine, absorbed as P, is oxidized in the thyroid and bound to a thyroglobulin. The resultant glycoprotein, mol wt 670,000, contains 120 tyrosine residues of which ca two-thirds are available for binding iodine in several ways. Proteolysis introduces the active hormones 3,5,3 -triiodothyronine (T ) and 3,5,3, 5 -tetraiodothyronine (T, (thyroxine) in the ratio Ty.T of 4 1 (121,122). 

Standardization and Testing". The final vaccine is tested for safety, potency, and residual chemicals. Safety includes testing for endotoxin and stetihty. Potency is evaluated by quantitative determination of the amount of hemagglutinin in the vaccine. Antibody to this glycoprotein is associated with protection. The single radial immunodiffusion (SKID) technique is used to standardi2e the mass of this protein in comparison to a reference preparation. 

Properties and Structure. a -Acid glycoprotein (a -AGP) has a molecular mass of about 41,000 and consists of a peptide chain having 181 amino acid residues and five carbohydrate units (14,15). Two cystine disulfide cross-linkages connect residues 5 and 147 and residues 72 and 164. The carbohydrate units comprise 45% of the molecule and contain siaUc acid, hexosamine, and neutral hexoses. In phosphate buffer the isoelectric point of the... 

Coagulation Factors II, III, VII, IX, X, XI, and Xlla fragments, thrombin, and plasmin are classified as serine proteases because each possesses a serine residue with neighboring histidine and asparagine residues at its enzymatically active site (Table 3). Factors II, VII, IX, and X, Protein C, Protein S, and Protein Z are dependent on the presence of vitamin K [84-80-0] for their formation as biologically functionally active procoagulant glycoproteins. 

A variety of cellular and viral proteins contain fatty acids covalently bound via ester linkages to the side chains of cysteine and sometimes to serine or threonine residues within a polypeptide chain (Figure 9.18). This type of fatty acyl chain linkage has a broader fatty acid specificity than A myristoylation. Myristate, palmitate, stearate, and oleate can all be esterified in this way, with the Cjg and Cjg chain lengths being most commonly found. Proteins anchored to membranes via fatty acyl thioesters include G-protein-coupled receptors, the surface glycoproteins of several viruses, and the transferrin receptor protein. 

FIGURE 9.26 The carbohydrate tnoiedes of glycoproteins may be linked to the protein via (a) serine or threonine residues (in the O-linked saccharides) or (b) asparagine residues (in the N-linked saccharides), (c) N-Linked glycoproteins are of three types high mannose, complex, and hybrid, the latter of which combines structures found in the high mannose and complex saccharides. 

Several drugs in current medical use are mechanism-based enzyme inactivators. Eor example, the antibiotic penicillin exerts its effects by covalently reacting with an essential serine residue in the active site of glycoprotein peptidase, an enzyme that acts to cross-link the peptidoglycan chains during synthesis of bacterial cell walls (Eigure 14.17). Once cell wall synthesis is blocked, the bacterial cells are very susceptible to rupture by osmotic lysis, and bacterial growth is halted. 

Concanavalin A is a plant lectin from the jack bean (Canavalia ensiformis) which binds with high affinity to mannose residues of glycoproteins. Concanavalin A is known to stimulate the tyrosine kinase activity of the INSR (3-subunit with consecutive activation of kinases downstream the insulin receptor (IRS, PI 3-kinase). It is believed that Concanavalin A stimulates the activation and autophosphorylation of the INSR kinase through aggregation of the receptor, although the precise mechanism of action is unclear. 

Oligosaccharide and polysaccharide structures occur not only in free form but often as parts of glycopeptides or glycoproteins [11] or of glycolipids [21]. It can be cumbersome to designate their structures by using the recommendations of 2-Carb-37. The use of three-letter symbols for monosaccharide residues is therefore recommended. With appropriate locants and anomeric descriptors, long sequences can thus be adequately described in abbreviated form. 

Polymers containing covalently bound monosaccharide and amino-acid residues are termed glycoproteins, glycopeptides or peptidogiycans. It is not possible to give... 

Influenza virus sialidase (Fig. 2) is a tetrameric glycoprotein consisting of four identical subnnits (Colman and Ward 1985), and acts as a glycohydrolase that removes a-ketosidically linked terminal AT-acetylneuraminic acid residues from gly-coconjugates. 

Fucose Deoxyhexose Fuc GDP-Fuc May be external in both N- and 0-linked glycoproteins or internal, linked to the GIcNAc residue attached to Asn in N-linked species. Can also occur internally attached to the OH of Ser (eg, in t-PA and certain clotting factors). 

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