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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Soluble glycoproteins have been purified from a series of clones of Trypanosoma brucei 427. Each clone yielded a characteristic predominant glycoprotein which induced clone-specific immunity to trypanosome infection in mice. These glycoproteins were shown by specific labelling and enzyme digestion of cells to be the major components of the trypanosome surface coat. Each glycoprotein consisted of a single polypeptide chain having an apparent molecular weight of 65 000 (as measured by SDS-polyacrylamide gel electrophoresis) and containing around 600 amino acid and 20 monosaccharide residues. Preliminary structural studies indicated large changes in amino acid sequence dispersed over a considerable length of the polypeptide chain. Proteolytic activity was demonstrated in semi-purified trypanosome extracts, providing one reason for the heterogeneity sometimes observed in surface glycoprotein antigen preparations.
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PMID:Identification, purification and properties of clone-specific glycoprotein antigens constituting the surface coat of Trypanosoma brucei. 0 Jun 45

We isolated an ether-resistant internal antigen and an ether-sensitive antigen previously described in relation to bovine leukemia virus infection. These two antigens have now been isolated by isoelectric focusing and concanavalin A affinity chromatography, respectively. The ether-resistant antigen exhibited isoelectric heterogeneity with a major peak at pH 7.2 and a minor peak at pH 6.2. Its molecular weight, estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), was 23,000 (p23), and it gave a sedimentation value of 2.3s. For material containing ether-sensitive antigen, analyzed by SDS-PAGE, protein staining revealed four components with molecular weights of 18,000, 25,000, 45,000, and 55,000. Two of these [45,000 (gp45) and 55,000 (gp55)] were stained by periodic acid-Schiff reagent. Isoelectric point and sedimentation value of the major glycoprotein (gp45) were pH 5.0 and 3.4s, respectively; no immunologic cross-reactivity was found between p23 and glycoprotein antigen.
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PMID:Properties of two isolated antigens associated with bovine leukemia virus infection. 1 Apr 47

Media of pig aorta was extracted with 1 M NaCl and 2 M MgCl2 to remove most of the soluble collagen, proteoglycans and glycoproteins. The glycoproteins remaining in the residue were extracted with 6 M urea-0.1 M mercaptoethanol. The urea soluble proteins were precipitated by dialysis, redissolved in 4 M guanidine-0.05 M DTT and were S-carboxamidomethylated (CM-guanidine extract). This extract was further fractionated by a variety of methods in order to separate a glycoprotein from collagen and proteoglycans. Caesium chloride density-gradient ultracentrifugation of the CM-guanidine extract separated a minor proteoglycan peak from a major glycoprotein fraction still containing some hydroxyproline. This major glycoprotein fraction was excluded as a single peak from Sephadex G 100 and G 200 in 4 M guanidinium chloride or in 6 M urea-0.2 per cent SDS. Sodium dodecylsulphate gel electrophoresis separated this high molecular weight Sephadex fraction into a major low molecular weight (approximately 35000 daltons) component and a minor high molecular weight component. This glycoprotein fraction could also be separated from a collagenous fraction and from proteoglycans by ion exchange chromatography on DEAE cellulose or by gelfiltration on Sepharose 4 B in 6 M urea-0.02 M EDTA-0.2 per cent SDS at pH 7.0. The isolated glycoprotein fraction is rich in dicarboxylic amino acids, contains galactose, mannose, (glucose), N-acetylglucosamine and sialic acid. The S-carboxamidomethyl glycoprotein preparation interacts with acid soluble calf skin collagen on isoelectric focusing in sucrose gradient in urea. This interaction is in favour of the biological role claimed for structural glycoproteins during fibrogenesis and differentiation.
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PMID:Structural glycoprotein from the media of pig aorta. Aggregation of the S-carboxamidomethyl subunits. 1 33

Efforts have been directed toward partial purification and identification of a reversible decapacitation factor from rabbit seminal plasma. Five fractions were consistently obtained following fractionation of rabbit seminal plasma on a Sephadex G-200 column. Only the first two fractions had decapacitation factor (DF) activity. On SDS polyacrylamide gel electrophoresis, several carbohydrate-and protein-containing components were found in each fraction from the Sephadex column. Further, DF activity could be obtained in the precipitate resulting from cetyl pyridinium chloride (CPC) treatment of the active fractions from the Sephadex G-200 column. In the comparison of the components observed with SDS gel electrophoresis throughout these fractionation procedures, the reversible decapacitation activity appeared to be associated with a component containing protein and carbohydrate. From these studies, then, reversible decapacitation activity of rabbit seminal plasma appears to be associated with a glycoprotein of an approximate molecular weight of 115,000.
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PMID:Partial purification and identification of a reversible decapacitation factor from rabbit seminal plasma. 4 14

An inhibitor of neutral subtilopeptidase [EC 3.4.24.4] was purified from porcine serum by salting out with (NH4)2SO4, chromatography on anion exchange sephadex, gel filtration with Sepharose 6B, and isoelectric focusing. The preparation was homogeneous by electrophoretic and ultracentrifugal criteria, and was shown to be a glycoprotein with a molecular weight of 740,000. It inhibited the caseinolytic activities of thermolysin, subtilisin, trypsin [EC 3.4.21.4], and alpha-chymotrypsin [EC 3.4.21.1] as well as that of neutral subtilopeptidase by an equimolar binding to those proteolytic enzymes. SDS-polyacrylamide gel electrophoresis after reduction with beta-mercaptoethanol indicated that the inhibitor was made up of four subunit monomers having a molecular weight of 190,000. From comparisons of its physiocochemical and inhibitory properties with those of well-investigated plasma proteins, the inhibitor was identified as alpha2-macroglobulin. On treatment of the inhibitor with neutral subtilopeptidase, a protein with a molecular weight of 95,000 appeared after treatment with SDS and beta-mercaptoethanol, suggesting that a peptide bond susceptible to the enzyme exists near the mid-point of the subunit chains.
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PMID:A neutral subtilopeptidase inhibitor from porcine serum some evidence for alpha2-macroglobulin. 5 60

A polar, nonpenetrating compound of high specific activity, diazotized (125I)-diiodosulfanilic acid (DD125ISA), has been developed as a label for exposed proteins of the human platelet plasma membrane, and platelet proteins and the pattern of labeling have been studied with sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). That DD125ISA binds specifically to membrane proteins was demonstrated by: (1) the specific activity of isolated membrane protein was five to seven times that of whole platelet protein and (2) no proteins of intact platelets were labeled which were not represented in the isolated plasma membrane. That the DD125ISA-labeled membrane proteins were exposed on the cell surface was demonstrated by: (1) DD125ISA-labeled proteins were altered by trypsin treatment of intact, labeled platelets and (2) the pattern of labeling produced by reaction of isolated membranes with DD125ISA was quite different from that produced by the labeling of intact platelets. Analysis of platelet membrane proteins by SDS-PAGE demonstrated the glycoproteins previously described at 150,000 daltons (termed glycoprotein I) and 92,000 daltons (glycoprotein III) but we could discriminate two apparently distinct glycoproteins in the intermediate region (IIa: 125,000 daltons, and II: 118,000 daltons). Glycoproteins I and III were constant whereas IIa was clearly visible only in unreduced samples and II was predominant in reduced samples. Reaction of DD125ISA with intact platelets resulted in equal labeling of three of these four membrane glycoproteins (IIa, II, and III). The pattern of exposed proteins on the platelet surface labeled by DD125ISA was different from lactoperoxidase-131I, which labeled predominantly the 92,000 dalton glycoprotein, as demonstrated by simultaneous SDS-PAGE analysis. Therefore three glycoproteins of the human platelet plasma membrane are exposed to a radioisotope probe on the platelet surface and are accessible for contact interactions.
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PMID:Studies on platelet plasma membranes. I. Characterization of surface proteins of human platelets labeled with diazotized (125i)-diiodosulfanilic acid. 6 Apr 57

Previous studies in this laboratory have shown that normal human serum contains an alpha globulin possessing lethal and antirespiratory action for staphylococci. In this study further description of the antistaphylococcal macromolecule is presented. The antistaphylococcal protein was shown to be homogeneous by both isoelectric focusing in sucrose density gradients and sodium dodecyl sulfate electrophoresis. An analysis of the chemical composition of the antistaphylococcal serum protein indicated the alpha globulin to be a glycoprotein composed of 22.5% carbohydrate and 77.2% protein as determined by amino acid analysis. The total carbohydrates included 11.08% protein-bound hexoses. 0.86% hexosamines, 4.3% sialic acid and 6.3% fucose. The mean isoelectric point, determined by isoelectric focusing in the range pH 3-6, was 4.73. Molecular weight studies on Sephadex G-200 dextran gel columns calibrated with proteins and glycoproteins indicated the molecular weight of the antistaphylococcal macromolecule to be 55,000-74,000 daltons respectively. SDS-gel electrophoresis indicated the molecular weight of antistaphylococcal serum protein was 62,000. Thus the antistaphylococcal alpha globulin does not appear to be related to other known serum bactericidins.
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PMID:Analysis of an antistaphylococcal serum alpha globulin. 7 43

A cell hybrid has been selected from fusion of a mouse myeloma and rat spleen cells immunized against mouse lymphoma cells that produces monoclonal antibody against the mouse lymphocyte surface glycoprotein, T200. Antibody binding assays employing the monoclonal antibody show that there are about 50,000-100,000 molecules of T200 glycoprotein on mouse thymocytes and that similar antigens are present on spleen and bone marrow but not detected on nonlymphoid tissues. Examination of the labeled molecules precipitated from detergent extracts of spleen cells and thymocytes iodinated by the lactoperoxidase technique by SDS-PAGE confirm that there are structural differences between the antigens found on B and T lymphocytes. The B-cell glycoprotein consists of at least one component of apparent mol wt 220,000 on SDS-PAGE, while the T-cell glycoprotein has an apparent mol wt of about 190,000.
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PMID:Interspecies spleen-myeloma hybrid producing monoclonal antibodies against mouse lymphocyte surface glycoprotein, T200. 7 61

The biochemical characteristics of immunoglobulin binding factor produced by activated cells (ATC) were investigated. For this purpose, supernatants of ATC were purified by affinity chromatography on insolubilized IgG and the eluted material was iodinated (125I), treated with mercaptoethanol; and run on SDS polyacrylamide gels. The radioactivity was found in two peaks corresponding to m.w. of 38,000 d and 18,000 d. This result extends and confirms our previous findings that IBF produced by ATC is identical to IBF produced by L-5178-Y internally labeled thymoma cells. The effect of various pH, temperatures, and proteolytic and glycolytic enzymes on the binding properties of 3H-leucine-or H-fucose-labeled IBF to IgG and on the polyacrylamide gel profiles was also studied. By all these criteria, IBF appeared to be a glycoprotein in which the presence of the 38,000 to 40,000 d chain is necessary for the binding to IgG. In the attempt to study the relationships between IBF and I-region products, purified IBF produced by ATC was incubated with anti-Ia immunoadsorbent, and the eluted material was iodinated and run on gels. The 38,000 d and 18,000 d chains characteristic of IBF were found to be specifically retained on the relevant immunoadsorbent. These data favor the hypothesis that IBF bears or is associated with Ia determinants.
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PMID:Characterization of suppressive immunoglobulin-binding factor (IBF). III. Biochemical and immunochemical characteristics of IBF produced by activated T cells. 7 16

Of the three major proteins associated with the rabies virus membrane, only the glycoprotein was found to be located on the external surface of the virus membrane. Glycoprotein prepared by treatment of rabies virus with Triton X-100 and purified by isoelectric focusing was found to be homogeneous with respect to size and isoelectric point. This material, which is free of phospholipids, is able to protect in vaccination experiments against a lethal challenge infection with rabies virus. The apparent mol. wt. of this component isolated under non-denaturing conditions is approx. 400000. The same material analysed by SDS polyacrylamide gel electrophoresis (PAGE) was found to consist solely of polypeptide chains of the G protein (mol. wt. 80000). A minor glycoprotein (gp 50), detected by PAGE of the Triton X-100 released material, appeared to be a breakdown product of the G-protein. Therefore the detergent released material represents homopolymers of the G-protein. Whether the antigenic determinants reside on the monomeric subunit or are a property of the polymeric form of the G-protein is discussed.
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PMID:Isolation and purification of a polymeric form of the glycoprotein of rabies virus. 8 Apr 43


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