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Protein sulfation

Protein sulfation occurs exclusively at tyrosine residues." It has been suggested that up to 1 % of the tyrosine protein content becomes sulfated, which is the most abundant posttranslational modification for tyrosine, with phosphorylation occurring only on 0.5% of tyrosine protein content." Sulfation occurs mostly on excreted proteins or trans-membrane proteins. Sulfation is catalyzed by tyrosylprotein sulfotransferase (TPST), with PAPS as a cosubstrate (Scheme 4). Like kinases, sulfotransferases have a biological inverse known as sulfatases." ... [Pg.442]

Scheme 4 Catalytic mechanism of protein sulfation. Tyrosine attacks electrophilic sulfur generating 3, 5 -ADP as a leaving group. Scheme 4 Catalytic mechanism of protein sulfation. Tyrosine attacks electrophilic sulfur generating 3, 5 -ADP as a leaving group.
D. The mucopolysaccharides of proteoglycans contain long chains of repeating disaccharide units that are covalently linked to a protein. Sulfation occurs after the monosaccharides are incorporated into the mucopolysaccharide chain. Proteoglycans are degraded by lysosomal... [Pg.315]

The cation concentration is equal to the sodium concentration plus that of unmeasured cations (UCs), predominantly magnesium, calcium, and potassium. The anion concentration is equal to the concentrations of chloride, bicarbonate, and unmeasured anions (UAs), including proteins, sulfates, phosphates, and organic anions. Therefore, as the result of the combination of the two equations above the SAG can be expressed as ... [Pg.987]

Some proteins, like gastrin, undergo sulfation by the addition of a sulfate group SO4 to the tyrosine residue in the protein. Sulfation is carried out by the action of two enzymatic steps mediated by two different transferases. [Pg.112]

P. A. Baeuerle, W. B. Huttner, Chlorate—a potent inhibitor of protein sulfation in intact cells. Biochem. Biophys. Res. Common. 1986 141, 870-877. [Pg.1373]

Affinity chromatography is used in the preparation of more highly purified Factor IX concentrates (53—55) as well as in the preparation of products such as antithrombin III [9000-94-6] (56,57). Heparin [9005-49-6], a sulfated polysaccharide (58), is the ligand used most commonly in these appHcations because it possesses specific binding sites for a number of plasma proteins (59,60). [Pg.529]

The sulfate groups are beUeved to be important in gelation with potassium and in reaction with protein. The 3,6-anhydrogalactose units increase hydrophobicity and reduce solubiUty whereas the sulfate groups increase hydropltilicity and solubiUty. [Pg.433]

Sulfur. Sulfur is present in every cell in the body, primarily in proteins containing the amino acids methionine, cystine, and cysteine. Inorganic sulfates and sulfides occur in small amounts relative to total body sulfur, but the compounds that contain them are important to metaboHsm (45,46). Sulfur intake is thought to be adequate if protein intake is adequate and sulfur deficiency has not been reported. Common food sources rich in sulfur are Hsted in Table 6. [Pg.378]

Metabolic Functions. Manganese is essential for normal body stmcture, reproduction, normal functioning of the central nervous system, and activation of numerous enzymes (126). Synthesis of the mucopolysaccharide chondroitin sulfate involves a series of reactions where manganese is required in at least five steps (127). These reactions are responsible for formation of polysaccharides and linkage between the polysaccharide and proteins that form... [Pg.386]

Fig. 3. Sodium dodecyl sulfate—polyacrylamide gel electrophoretic pattern for molecular weight standards (lane 1) water-extractable proteins of defatted soybean meal (lane 2) purified IIS (glycinin) (lane 3) and purified 7S (P-conglycinin) (lane 4) where the numbers represent mol wt x 10. The gel was mn in the presence of 2-mercaptoethanol, resulting in the cleavage of the disulfide bond linking the acidic (A bands) and basic (B bands) polypeptides of the... Fig. 3. Sodium dodecyl sulfate—polyacrylamide gel electrophoretic pattern for molecular weight standards (lane 1) water-extractable proteins of defatted soybean meal (lane 2) purified IIS (glycinin) (lane 3) and purified 7S (P-conglycinin) (lane 4) where the numbers represent mol wt x 10. The gel was mn in the presence of 2-mercaptoethanol, resulting in the cleavage of the disulfide bond linking the acidic (A bands) and basic (B bands) polypeptides of the...
Tofu. Tofu is prepared by adding a coagulant such as calcium sulfate to soymilk to precipitate the protein and oil into a gelatinous curd. The curd is then separated from the soluble portion (whey), pressed, and washed to yield a market-ready product. Tofu, a traditional food in Japan (90), was populari2ed in the United States in the late 1970s and is available in many U.S. supermarkets. [Pg.304]

Nutrition. Zinc is essential to the proper functioning of plants and animals and, as zinc sulfate and oxide, it is used as a feed supplement (49—51) (see Mineral nutrients Feedsand feed additives). Most crops use less than a kilogram of zinc per 1000 m per year, so that zinc salts added at 1.3—4.5 kg/ha gradually build up the zinc reserve (52). Animals, including humans, store relatively Htde available zinc and, thus, require a constant supply in the diet. For instance, beef cattle require 10—30 mg/kg dry feed, dairy cattle 40 mg/kg, and breeding hens 65 mg/kg. Zinc from plants is considered less available to monogastric aminals than zinc from animal protein. [Pg.423]

Some polymyxins are sold for second-line systemic therapy. Polymyxin B sulfate and colistimethate sodium can be used for intravenous, intramuscular, or intrathecal administration, especially for Pseudomonas aerupinosa mP QXiosis, but also for most other gram-negative organisms, such as those resistant to first-line antibiotics. Nephrotoxicity and various neurotoxicities are common in parenteral, but not in topical, use. Resistance to polymyxins develops slowly, involves mutation and, at least in some bacteria, adaptation, a poorly understood type of resistance that is rapidly lost on transfer to a medium free of polymyxin. Resistance can involve changes in the proteins, the lipopolysaccharides, and lipids of the outer membrane of the cell (52). Polymyxin and colistin show complete cross-resistance. [Pg.149]

About 97% of po dose is absorbed from the GI tract. The dmg undergoes extensive first-pass hepatic metaboHsm and only 12% of the po dose is bioavailable. More than 95% is protein bound and peak plasma concentrations are achieved in 2—3 h. Therapeutic plasma concentrations are 0.064—1.044 lg/mL. The dmg is metabolized in the Hver to 5-hyroxypropafenone, which has some antiarrhythmic activity, and to inactive hydroxymethoxy propafenone, glucuronides, and sulfate conjugates. Less than 1% of the po dose is excreted by the kidney unchanged. The elimination half-life is 2—12 h (32). [Pg.114]


See other pages where Protein sulfation is mentioned: [Pg.258]    [Pg.443]    [Pg.127]    [Pg.774]    [Pg.764]    [Pg.1306]    [Pg.206]    [Pg.258]    [Pg.443]    [Pg.127]    [Pg.774]    [Pg.764]    [Pg.1306]    [Pg.206]    [Pg.1121]    [Pg.1121]    [Pg.457]    [Pg.55]    [Pg.61]    [Pg.366]    [Pg.466]    [Pg.476]    [Pg.459]    [Pg.154]    [Pg.243]    [Pg.513]    [Pg.497]    [Pg.228]    [Pg.27]    [Pg.99]    [Pg.133]    [Pg.202]    [Pg.360]    [Pg.8]    [Pg.127]    [Pg.181]    [Pg.530]    [Pg.71]    [Pg.459]    [Pg.181]   
See also in sourсe #XX -- [ Pg.30 , Pg.34 ]

See also in sourсe #XX -- [ Pg.114 , Pg.115 ]

See also in sourсe #XX -- [ Pg.112 ]




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Ammonium sulfate protein fractionation

Carbohydrate-protein linkage region chondroitin sulfate

Chondroitin sulfate, carbohydrate-protein

Chondroitin sulfate, carbohydrate-protein linkage

Chondroitin sulfate-protein

Chondroitin sulfate-protein carbohydrate sequence

Chondroitin sulfate-protein complex, biosynthesis

Denaturation of proteins by sodium dodecyl sulfate

Dermatan sulfate-protein

Halistanol sulfate pp60v-src protein tyrosine kinase

Heparan sulfate matrix proteins

Heparin sulfate interactions with proteins

Iron-sulfur proteins in sulfate-reducing bacteria

Keratan sulfate carbohydrate-protein linkage

Protein separation with ammonium sulfat

Protein sulfate esters

Simple and Complex Iron-Sulfur Proteins in Sulfate Reducing

Simple and Complex Iron-Sulfur Proteins in Sulfate Reducing Bacteria

Sodium dodecyl sulfate protein complex

Sulfate binding protein

Sulfate binding protein active site

Sulfate esters in proteins

Sulfate-reducing bacteria iron-sulfur proteins

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