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Query: UMLS:C0272170 (SDS)
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Cell surface molecules of rat normal lymphoid cells were selectively labelled by lactoperoxidase catalysed iodination or by a galactose oxidase tritiated sodium borohydride technique, subsequently detergent solubilized, isolated by indirect immunoprecipitation and analysed on SDS-polyacrylamide gel electrophoresis. Four polypeptide chains were isolated by using the alloantiserum DA anti-Lewis. The molecular weights of the antigens were calculated as 41,000, 33,000, 27,000 and 12,000. Based on functional in vitro characteristics of the antiserum used and on the physiochemical properties as well as genetics of inheritance and tissue distribution, the polypeptide chains were identified as being subunits of Ag-B and Ia antigens. Two types of immunoglobulin heavy chains exhibiting the molecular weight 70,000 and 64,000 were isolated from unfractionated normal spleen cells by use of a polyvalent rabbit anti-rat immunoglobulin serum and tentatively identified as mu and delta chain. Using the same anti-immunoglobulin serum, no molecules could be precipitated from the lysated of Lewis thymocytes or peripheral T cells.
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PMID:Isolation and partial characterization of rat lymphoid cell surface histocompatibility antigens and immunoglobulins. 41

The structural polypeptides of two strains of measles virus grown in Vero cells were analysed in SDS-PAGE slab gels. Six major polypeptides were identified with mol. wt. of 79000, 72000, 60000, 43000, 40000 and 36000. The largest polypeptide was sensitive to trypsin digestion and was the dominant glycosylated polypeptide identified when the virus was grown in medium containing 3H-fucose or 3H-glucosamine or when the virus was treated with galactose oxidase and labelled with 3H-sodium borohydride. It is concluded that the 79000 mol. wt. polypeptide represents the haemagglutinin. Treatment with non-ionic detergent removed this polypeptide and also the 40000 mol. wt. polypeptide from the virus envelope. The 40000 mol. wt. polypeptide is probably associated with haemolysin and cell fusion activities and is analogous to the F1 of paramyxoviruses. A polypeptide of mol. wt. approx. 20000 detected after glycoprotein labelling may represent the F2 of measles virus. The 43000 mol. wt. polypeptide co-migrates with cellular actin and is the only major measles polypeptide that is heavily labelled when the virus is grown on Vero cells prelabelled with 35S-methionine. Thus it may represent cellular actin incorporated into the virus during maturation. The quantity of the 72000 mol. wt. polypeptide relative to the other major polypeptides varied considerably in different virus preparations. The role of the polypeptide could not be defined. By analogy with previously published data the 60000 and 36000 mol. wt. polypeptides are inferred to represent nucleocapsid and membrane proteins, respectively.
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PMID:Structural polypeptides of measles virus. 65 Jan 74

Specific anti-Ly sera were employed to precipitate Ly antigens from Nonidet P-40 extracts of mouse thymocytes labeled with 125I using lactoperoxidase and with NaB3H4 using galactose oxidase. Thymocytes from mice of the congenic strains C57BL/6J (Ly-2.2, Ly-3.2 positive), C57BL/6Ly-2a, Ly-3a (Ly-2.1, Ly-3.1 positive) and C57BL/6-Ly-2a (Ly-2.1, Ly-3.2-positive) were used as sources of labeled antigens and as immune adsorbants to permit evaluation of the specificity of each anti-Ly serum employed. Results of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions are consistent with the Ly-3.1 antigen containing a glycoprotein subunit with an apparent mol wt of 35,000 daltons. Specific precipitates obtained using anti-Ly-2.1 serum yielded SDS-PAGE profiles identical to that obtained with anti-Ly-3.1 serum, suggesting that the Ly-2 and Ly-3 antigens have the same molecular weight distribution. The relationships of these results to the observed close genetic and topological linkage of Ly-2 and Ly-3 and to the genetic linkage of these loci with the IB-peptide marker, a mouse Bk-region polymorphism, are discussed.
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PMID:The Ly-3 antigens on mouse thymocytes: immune precipitation and molecular weight characterization. 82 15

Analysis of synaptosomal plasma membrane from mouse brain by SDS gel electrophoresis reveals a large number of glycoprotein and glycolipid species, as distinguished by periodic acid Schiff or by the distribution of in vivo incorporated 3H-fucose label. The topographical distribution of this carbohydrate in the plasma membrane was examined by labelling intact synaptosomes and isolated membrane with galactose oxidase (E.C. 1.1.2.9.)-3H-NaBH4. In both, gangliosides and a wide spectrum of glycoprotein species were labelled. Extraction of SPM with 0.05 N NaOH at 0 degrees C removed about two-thirds of the membrane's protein. Gel electrophoresis of the solubilized material revealed partial or complete extraction of a large number of polypeptide species; however, all of the glycoproteins, as well as the glycolipid, remained in the insoluble pellet. These results indicate a highly asymmetric arrangement of glycoproteins and glycolipids in SPM; most or all of these species reside on the external surface of the synaptosome, accessible to galactose oxidase. The glycoproteins appear to be more deeply-buried in the lipid bilayer than the other polypeptide species, as has been found in other systems.
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PMID:The organization of carbohydrate in mouse synaptosomal plasma membrane. 92 42

The composition and disposition of the constituent polypeptides of rat cerebral cortical synaptosomal membranes were analyzed on SDS acrylamide gels. Of 20 bands readily detected, 11 account for greater than 93% of the total protein analyzed. These are: (molecu25); 3 (175); 4 (doublet, 137); 5 (doublet, 97); 6 (68); 7 (61); 8 (54); 9 (44); 10 (37); and 11 (33). Bands 5 and 8-10 are the most prominent and account for greater than 60% of the protein mass or 0.67 of its molecular fraction. By lactoperoxidase iodination, the bulk of the proteins in bands 3, 5, 6, and 8 and a portion of band 11 appear to be located on the external (junctional) face of the membrane of intact synaptosomes; proteins in bands 1, 2, 7, 9, and 10 appear to be localized on the internal (synaptoplasmic) face and become labeled only when synaptosomes are lysed. Further confirmation of the topographical distribution is provided by evidence that bands 3-6, 8, and 11 contain glycoproteins susceptible to labeling in intact synaptosomes by oxidation with galactose oxidase or periodate followed by reduction with NaB3H4. Evidence is provided for significant contributions by tubulin- and actin-like molecules to bands 8 and 9, respectively, suggesting that a substantial fraction of the tubulin in the synaptosomal membrane is disposed externally (accessible to iodination) whereas most, if not all, of the actin appears to exhibit the opposite topography. Similar though weaker inferences can also be drawn with regard to the location of tropomyosin and troponin. Preliminary evidence is provided that postsynaptic densities exhibit a protein and iodination profile distinct from that of the synpatosomal membrane.
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PMID:Topography of the synaptosomal membrane. 103 85

A simple method for the release of oligosaccharides from glycoproteins separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) has been developed. Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound. After electrophoretic separation of the glycoprotein, oligosaccharides were released by the use of a gas-phase hydrazinolysis apparatus. In the first method, the gel was stained with Coomassie Blue and the glycoprotein together with the gel was directly subjected to gas-phase hydrazinolysis after removal of water in a P2O5 desiccator. The recovery of released oligosaccharides was 25.9 +/- 2.4%, based on the amount of the glycoprotein loaded on the gel within the range of 3.5-28.5 micrograms. In the second method, the glycoprotein was electroblotted onto an Immobilon transfer membrane and was visualized by staining with Coomassie Blue. A small piece of the membrane with the corresponding band was cut out, dried in a desiccator and subjected to gas-phase hydrazinolysis. In this case, the recovery of released oligosaccharides was 15.2 +/- 1.0%. These procedures, particularly the first one, should be widely applicable for the isolation of oligosaccharides from glycoproteins separated by SDS-PAGE.
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PMID:A simple method for the release of asparagine-linked oligosaccharides from a glycoprotein purified by SDS-polyacrylamide gel electrophoresis. 163 58

Human lung adenocarcinoma sub-cell lines HAL-8, HAL-24 and HAL-33, showing different lung colonization potential (LCP), were established from human lung adenocarcinoma cell line KUM-LK-2 using repeated cloning with limiting dilution technique. Cell lines HAL-8 and -33 were characterized by high and low LCP, respectively, while HAL-24 did not give rise to lung colonies. The cell surface protein and carbohydrate profiles were determined by cell surface labeling (with lactoperoxidase-dependent 125I-iodination and galactose oxidase-NaB3H4, respectively) followed by SDS-gel electrophoresis. Various carbohydrate epitopes expressed at the cell surface were analysed by cytofluorometry using various monoclonal antibodies (MAbs) directed to Le(x), sialosyl-Le(x), sialosyl dimeric Le(x), T, Tn and sialosyl-Tn structures, which are often reported as being highly expressed in a variety of human cancers, particularly adenocarcinoma. Expression of sialosyl dimeric Le(x) (defined by MAb FH6) was high on HAL-8, moderate on HAL-33, and relatively low on HAL-24. In contrast, each of the three lines showed essentially equal expression (as determined by MAb reactivity) of sialosyl-Tn (defined by MAb TKH2), Le(x) (defined by MAb SH1), and Tn (defined by MAb 1E3). The cell lines showed extremely weak expression of T (defined by MAb HH8). LCP of HAL-8 and -33 was completely inhibited by sialidase treatment of cells. It is suggested that higher expression of sialosyl dimeric Le(x) (defined by MAb FH6) in HAL-8 cells may play an important role in higher potential of blood-borne lung colonization.
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PMID:Human lung adenocarcinoma cell lines with different lung colonization potential (LCP), and a correlation between expression of sialosyl dimeric Le(x) (defined by MAb FH6) and LCP. 167 53

Rhodopsin's oligosaccharide chains contain predominantly two types of sugar residues: mannose and N-acetylglucosamine. In the present work, bovine and rat rhodopsin were analysed biochemically for the presence of a third sugar, galactose. Treatment of bovine rod outer segments (ROS) with galactose oxidase followed by reduction with tritium-labeled sodium borohydride revealed the presence of existing molecules of galactose on rhodopsin. Rats injected intravitreally with [3H]galactose and [14C]leucine and maintained in darkness were killed 1 hr, 6 hr, 1, 3 or 5 days following the injection. Retinas were collected for subcellular fractionation and rhodopsin from each of the fractions was purified by ConA sepharose chromatography and SDS-PAGE. During the first 6 hr, galactose selectively labeled rhodopsin in the Golgi-enriched fraction resulting in increased [3H]/[14C] ratios in both Golgi and ROS. The data suggested that trimming was occurring at the transition from Golgi to ROS. Furthermore, a decrease in isotope ratio in the ROS between 6 hr and 1 day suggested further trimming of rhodopsin after membrane assembly in the ROS. Additional in vivo experiments demonstrated existing molecules of galactose on rhodopsin's oligosaccharide chain using lectin affinity chromatography. Rats injected intravitreally with [35S]methionine were dark-adapted for 2 hr. Following subcellular fractionation of retinas, ConA purified rhodopsin from ROS was applied to one of two additional lectin columns: Ricinus communis agglutinin (RCA) or Griffonia simplicifolia I (GSA). Eight to nine percent of the labeled rhodopsin was bound to and eluted from RCA, whereas none bound to GSA, indicating the presence of a beta-galactoside. The RCA agarose eluted protein co-electrophoresed with a rhodopsin standard and was light sensitive. Galactose was shown to be the terminal sugar on this subset of rhodopsin and was not capped by neuraminic acid. Binding of rhodopsin's oligosaccharide to RCA was abolished by pre-treatment with beta-galactosidase. Decreased binding of rhodopsin to RCA was observed following intravitreal injection of castanospermine but not swainsonine. Of those two inhibitors of glycoprotein trimming, only castanospermine would be expected to prevent the addition of galactose to the oligosaccharide. The association of galactose with rat rhodopsin appeared to be a transient one. At 2 hr, 8-9% of rhodopsin contained galactose, at 6 hr only 2.2% had galactose and by 24 hr less than 1% did. The galactose was trimmed from rhodopsin's oligosaccharide presumably after its role was complete. Separation of rhodopsin of the plasma membranes from rhodopsin of discs indicated that 75% of the galactose-containing rhodopsin was in the plasma membrane and only 25% was in the discs. These findings suggested a possible role for galactose in new disc formation with subsequent removal after the discs are sealed.
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PMID:Transient hyperglycosylation of rhodopsin with galactose. 193 88

Several murine monoclonal antibodies (MoAbs) were made to a family of human cytomegalovirus (HCMV) disulfide linked glycoprotein complexes designated gC-II. Characterization of these MoAbs by immunological methods showed that they could be divided into two groups recognizing different glycoproteins. Western blot analysis was done with immunoaffinity purified gC-II complexes. Under non-reducing conditions MoAbs from both groups recognized gC-II complexes with molecular weights of 67-93 k and 130 k to greater than 200 k. When purified gC-II complexes were reduced and individual glycoproteins separated by SDS-PAGE prior to Western blotting, Group 1 MoAbs reacted with glycoproteins having molecular weights of 47-63k, while Group 2 MoAbs reacted with glycoproteins having molecular weights of 39-48k and 90k to greater than 200k. Thus, gC-II complexes contain glycoproteins recognized by both groups of MoAbs. By Coomassie blue staining and incorporation of [3H]Arg, Group 1 glycoproteins appeared to be minor components in the complexes relative to Group 2 glycoproteins. Surface labeling of extracellular virus with galactose oxidase and tritiated borohydride showed that gC-II complexes of all molecular weights were on the surface of the virus. However, the most heavily labeled gC-II glycoproteins had molecular weights of 47-63k. These data confirm our previous observations that the gC-II complexes of HCMV are comprised of a heterogeneous family of glycoproteins.
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PMID:Characterization of cytomegalovirus glycoproteins in a family of complexes designated gC-II with murine monoclonal antibodies. 216 76

The ability of von Willebrand factor protein (vWF) to agglutinate platelets with ristocetin depends upon the presence of its highest molecular weight multimers (HMWM) and its intact carbohydrate structure. Previously we demonstrated that the HMWM are preferentially adsorbed to purified fibrillar type I collagen. The role of the carbohydrate structure of vWF in this function has not been established. In these studies complete desialylation (greater than 95%) of the intact protein by neuraminidase did not interfere with the normal adsorption of vWF activity to type I collagen. In contrast, modification of the penultimate galactose of the desialylated protein with galactose oxidase or beta-galactosidase markedly reduced adsorption of vWF activity by collagen. Subsequent reduction of the oxidized desialylated protein with potassium borohydride completely regenerated the normal adsorption of vWF activity by collagen. Enzymatic modification of the penultimate galactose moiety of vWF resulted in a loss of the HMWM, as observed following SDS-glyoxyl agarose electrophoresis. This was in contrast to desialylated vWF, which appeared intact structurally and which predictably lost its HMWM upon exposure to collagen in a manner similar to native vWF. Therefore, the carbohydrate structure of vWF and, in particular, the penultimate galactose moiety, may be critical for vWF-collagen interactions and for the mediation of primary hemostasis.
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PMID:Critical role of the carbohydrate moiety in human von Willebrand factor protein for interactions with type I collagen. 230 Sep 25


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