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

Anti-TF agglutinins from peanut (Arachis hypogaea) and from vertebrate sera of different species have been successfully isolated by affinity chromatography on acid-activated Sepharose 4 B. The proteins were characterized by immunoelectrophoresis, polyacrylamide gel electrophoresis in the presence of SDS and with respect to their carbohydrate binding specificities. Anti-TF substances from sera showed one precipitin arc in immunoelectrophoresis, but quantitative immunoprecipitation revealed our human anti-TF to be a mixture of the three Ig-classes IgG, IgA and IgM. This finding was confirmed on SDS gel electrophoresis, where high molecular weight aggregates were found before reduction. Hemagglutination inhibition revealed that all isolated anti-TF compounds exhibit an exceptionally high affinity for the immunodominant group of the TF-antigen, namely the beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosamine disaccharide. On examination of formalin-fixed and neuraminidase treated tissue sections (kidney, mammary gland), fluorescein-labelled anti-TF from horse serum showed a virtually identical pattern when compared with fluorescein labelled peanut lectin. Likewise isolated IgA-class myeloma J 539, which shows specificity against beta-(1 leads to 6)-galactans, only bound to the appropriate Gal-beta-(1 leads to 6)-Gal structures, such as those found on bovine lung or the albumin gland of Helix pomatia. Rabbit anti-VCN (Vibrio cholerae neuraminidase) activity could be selectively abolished by beta-galactosyl-containing inhibitors, whereas papain F(ab) fragments from rabbit anti-VCN immunoglobulin did not compete with anti-TF for binding sites on VCN-treated human red cells. Anti-TF, on the other hand, did not compete with anti-VCN for active VCN.
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PMID:Isolation, characterization and implications of anti-TF (Thomsen-Friedenreich) agglutinins from different sources. 615 37

[3H]N-acetylgalactosamine injected into the cell body of R2, the giant cholinergic neuron in the abdominal ganglion, is rapidly incorporated into membrane glycoprotein and glycolipid. Incorporation, which is localized to the injected cells, occurs at a constant rate for approximately 15 h. By that time, 83% of the labeled macromolecules are associated with membranes. Quantitative electron microscopic radioautography of the cell body shows that labeling of membranous organelles is selective: the Golgi apparatus, endoplasmic reticulum, and lucent and compound vesicles are labeled, while the nucleus, end-stage lysosomes, and mitochondria are not. SDS-polyacrylamide gel electrophoresis of the total membranes from more than 40 R2s examined individually resolves reproducibly 5 major labeled glycoprotein components. In order to determine which of these area associated with vesicles, we isolated a labeled vesicle fraction from R2 using a combination of differential centrifugation and filtration on a column of glass beads with 200 nm pores. This fraction was consistently enriched in [3H]glycoproteins I (180,000 Daltons) and V (90,000 Daltons) relative to those fractions containing larger organelles. These experiments suggest that different organelles contain characteristic membrane components.
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PMID:Distribution of membrane glycoproteins among the organelles of a single identified neuron of Aplysia. I. Association of a [3H]glycoprotein with vesicles. 616 24

Sialoglycoprotein which exhibits inhibitory activity for hemagglutination by Hemagglutinating Virus of Japan (HVJ, Sendai virus) was isolated from the membrane of bovine erythrocytes. Purification steps for this sialoglycoprotein included extraction with lithium diiodosalicylate, phenol partition, precipitation with ethanol, and chromatography on a phosphocellulose column and an SDS-Sepharose CL-4B column. Purified sialoglycoprotein (GP-2) has high specific activity for inhibiting the hemagglutination with HVJ, and a lesser activity for that with Newcastle disease virus, but it does not inhibit the hemagglutination by influenza A virus. Inhibitory activity of GP-2 on hemagglutination by HVJ is 2,500-fold higher than that of fetuin. Liposomes containing a 10,000-fold larger amount of ganglioside mixture of bovine erythrocytes and those containing a 5,000-fold larger amount of each ganglioside of bovine erythrocytes, N-glycolylneuraminosyl-lactosyl ceramide, sialosyllacto-N-neotetraosyl- and sialosyl-lacto-N-norhexaosyl ceramide, had no inhibitory activity toward hemagglutination with HVJ. GP-2 (mol. wt. 250 K daltons) behaved homogeneously in SDS-polyacrylamide gel electrophoresis. It contained 70% carbohydrate and 30% protein, by weight. N-Acetylgalactosamine, N-acetylglucosamine, galactose, sialic acid (N-glycolylneuraminic acid, 96%; N-acetylneuraminic acid, 4%) were identified as carbohydrate components, in molar ratios of 1.0:4.0:5.2:2.9. All the oligosaccharides of GP-2 appeared to be linked to polypeptide chains by alkali-labile O-glycosidic linkages. Sialidase treatment of GP-2 and conversion of sialic acid residue of the glycoprotein to C8 and C7 analogues resulted in the loss of the inhibitory activity on hemagglutination by HVJ. Oligosaccharides isolated by gel filtration after treatment of GP-2 with alkaline borohydride had also lost the ability to inhibit the hemagglutination by HVJ. The above results indicate that isolated sialoglycoprotein is the endogenous receptor in bovine erythrocyte membrane specific to HVJ, and the hydroxy group linked to the 9-carbon atom of sialic acid and probably also the hydrophobic protein moiety are important for the recognition of HVJ attachment.
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PMID:Isolation and characterization of receptor sialoglycoprotein for hemagglutinating virus of Japan (Sendai virus) from bovine erythrocyte membrane. 630 60

Casein of cynomolgus monkey was compared with those from human and bovine milk. Cynomolgus monkey casein showed similar electrophoretical patterns to those of human casein on Disc- and SDS-electrophoresis. It consisted of beta- and kappa-casein-like components. The component corresponding to bovine alpha s1-casein was not detected. The beta-casein-like fraction of cynomolgus monkey showed 9 bands on Disc-PAGE. These were suggested to be the same protein binding different levels of phosphorus by dephosphorylation experiment using an acid phosphatase. The kappa-casein-like component of cynomolgus monkey was highly glycosylated (about 50% carbohydrate) similarly as human kappa-casein and the constituent carbohydrates were same as those detected in human kappa-casein (galactose, fucose, N-acetylgalactosamine, N-acetylglucosamine, and sialic acid). Amino acid composition of cynomolgus monkey kappa-casein bore a resemblance to those of both human and bovine kappa-caseins. Amino acid composition of cynomolgus monkey beta-casein was also similar to those of human and bovine beta-caseins.
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PMID:Comparison of casein of cynomolgus monkey (Macaca fascicularis) with human casein. 640 2

JAR malignant trophoblast cells produce a free alpha subunit in addition to an alpha combined with beta subunit as hCG. The free alpha is larger by gel chromatography and SDS-PAGE than combined alpha and is unable to associate with beta subunit to form hCG. A tryptic fragment, representing amino acid residues 36-42, derived from free alpha was larger than the corresponding fragment from combined alpha. After neuraminidase treatment, the fragment from free alpha bound peanut lectin agarose, which is specific for Gal beta 1-3GalNAc as found in O-linked oligosaccharides. The fragment also contained Gal and GalNAc (and a lesser amount of GlcNAc) as determined by glycosidase sensitivity and amino sugar analyses. Removal of this tryptic fragment ablated the size difference between free and combined alpha subunits.
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PMID:An oligosaccharide of the O-linked type distinguishes the free from the combined form of hCG alpha subunit. 647 61

A further study has been made on the house dust mite extract, Dermatophagoides pteronyssinus, with emphasis on gel-filtrated fraction 2 (F2). The crude mite extract showed at least nine discs on polyacrylamide disc electrophoresis and contained less than 0.25% sialic acid and less than 0.5 mM hexosamine and no detectable uronic acid. From gel filtration of the crude extract a No 2 fraction (F2) with allergenic activity showed at least five components on SDS disc electrophoresis covering a molecular weight range of between 15,000 and 70,000. The major allergenic activity of F2 dissolved in pH 7-8 and 4-5 on an isoelectric focusing column. Affinity chromatography and lectins showed that allergenic activity did not relate to structures of N-acetyl-D-glucosamine or N-acetyl-D-galactosamine. Allergenic activity of the crude extract was no affected by peptic digestion and the mite digest prepared by trypsin and pronase showed a similar fractionation and activity profile as crude extract.
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PMID:Biochemical and allergenic properties of the house dust mite extract, Dermatophagoides pteronyssinus. 675 29

Milk fat globule membrane (MFGM) enclosing fat droplets in human milk was found to contain a high molecular weight glycoprotein which did not migrate in 10% acrylamide gel on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). This glycoprotein (termed PAS-0) was isolated by Sepharose CL-4B chromatography. Isolated PAS-0 gave one band on SDS-PAGE using 5% acrylamide gel (acrylamide : bisacrylamide = 4 : 1, w/w) and gave one peak on analytical ultracentrifugation, indicating its homogeneity. PAS-0 was rich in serine, threonine, proline, glycine, and alanine. In contrast, contents of sulfur-containing amino acids were very low. Fucose, galactose, N-acetylglucosamine, N-acetylgalactosamine, and sialic acid were detected as constituent sugars of PAS-0 and the total carbohydrate content was about 50%. Alkali-borohydride treatment suggested that the carbohydrate moiety was linked to the polypeptide core with O-glycosidic bond(s). There results suggested that PAS-0 was a mucin-like glycoprotein. PAS-0 was shown to be resistant to pepsin, trypsin and chymotrypsin digestion, but susceptible to Pronase and Subtilisin BPN'. Extraction of intact milk fat globules (cream) with MgCl2 and guanidine hydrochloride solutions suggested that PAS-0 was an intrinsic component of MFGM. Digestion of cream with Subtilisin BPN' demonstrated that PAS-0 was located on the external surface of fat globules and was accessible to molecules outside the globules. By agglutination-inhibition tests using eight lectins, PAS-0 was suggested to act as surface receptors for Ricinus communis agglutinin, wheat germ agglutinin and peanut agglutinin.
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PMID:Isolation and characterization of mucin-like glycoprotein in human milk fat globule membrane. 706 73

A major cell surface sialoglycoprotein with Concanavalin A receptor activity has been isolated from rat Zajdela ascites hepatoma cells. The sialic acid residues of the plasma membrane glycoproteins were specifically labeled by oxidation and NaIO4 followed by reduction with NaB3H4. Surface-labeled glycoproteins were released by short incubations with TPCK-trypsin at 37 degrees C and then separated by gel filtration on Sepharose 6B column. The predominantly labeled fraction, GP II2, was then purified by chromatography on DEAE-cellulose equilibrated with 0.05 M phosphate buffer, pH 7.5, and eluted with increasing molarities of NaCl. It was shown to be homogeneous by protein and carbohydrate staining on SDS-polyacrylamide gels, isoelectric focusing, rechromatography on DEAE-cellulose and immunoelectrophoresis. It has an apparent molecular weight of 110,000 daltons. The location of GP II2 on the cell surface was confirmed by the fact that it could be labeled metabolically with D-(3H) glucosamine and externally through the nonpenetrating periodate-NaB3H4 system. GP II2 could not be removed from the cell surface by high salt concentrations, chelator, or chaotropic agents but was released from the membrane by detergents. This suggests that GP II2 could be an integral protein. Analysis of the carbohydrate composition of GP II2 revealed galactose, N-acetylglucosamine, N-acetylgalactosamine, and sialic acid as major constituents and mannose as a minor one. This suggests that it contains carbohydrate chains both O- and N-linked to the polypeptide chain, most of them being O-linked. Finally, GP II2 has a potent Concanavalin A receptor activity. It inhibits the interaction between Concanavalin A and hepatoma cells and suppresses its effects on hepatoma cell proliferation.
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PMID:Purification and characterization of a major cell surface glycoprotein in Zajdela ascites hepatoma cells which displays a potent concanavalin A receptor activity. 706 81

Neurons are highly differentiated cells whose various regions must differ in macromolecular composition. This is demonstrated in the present study which shows that specific membrane glycoproteins are routed to particular sites in the cell. When [3H]fucose of [3H]N-acetylgalactosamine are injected into R2, the giant neuron of Aplysia, they are incorporated into relatively few glycoproteins, several of which can be readily identified from cell to cell. Because R2's cell body is so large, its surface membrane can be isolated 94% free of cytosol by manual dissection. The purity of the membrane was assessed by checking the distribution of the enzyme choline acetyltransferase. R2's axon can also be analyzed separately from the cell body. At 24 h after injection, SDS polyacrylamide gel electrophoresis shows that glycoprotein-I (mol. wt. 180,000) is the major labeled component of the external membrane where it is enriched relative to the content of the other cytosolic membranes. In contrast, glycoprotein-V (mol. wt. 90,000) predominates among the membranes of the axon. The disposition of glycoprotein-I in the external membrane was indicated by exposing R2 to low concentrations of pronase in situ 24 h after injection. Labeled glycopeptides were released from R2's surface and gel filtration and high voltage electrophoresis indicated that some of these were derived from glycoprotein-I. Examination of the isolated surface membrane after proteolysis showed a reduced amount of labeled glycoprotein-I. Consistent with these findings, a glycoprotein of similar molecular weight as component-I was labeled when R2 was treated with galactose oxidase and potassium borotritide. These results indicate that the carbohydrate moieties of glycoprotein-I extend from R2's surface.
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PMID:Differences in the distribution of specific glycoproteins among the regions of a single identified neuron. 709 98

A low-molecular-weight, monomeric, mucin-type glycoprotein (MG2) has been isolated from human submandibular-sublingual saliva. Initial purification involved sequential gel-filtration on Sephadex G-200 and Sepharose CL-2B, the latter in the presence of 6M urea. Fractions containing MG2 were next separated from contaminating secretory IgA by immunoaffinity chromatography or recycling through Sephadex G-200. Mucin fractions were 14C-labeled by reductive methylation, and then the final purification-step entailed recycling radiolabeled materials through Sephadex G-200. Radiolabeling aided in the assessment of purity, as judged by SDS-PAGE and ion-exchange chromatography. The carbohydrate portion accounted for 69.6% of the recovered weight and was composed of N-acetyl-glucosamine, N-acetylgalactosamine, galactose, fucose, and N-acetylneuraminic acid. Sulfate was also present. The protein comprised 30.4% of the recovered weight with threonine, serine, proline, and glycine accounting for 75.2% of the total amino acids. The oligosaccharides were alkali-labile, indicating an O-glycosyl linkage to the peptide. The mucin was weakly acidic and had an estimated mol. wt. of 200 000-250 000.
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PMID:Purification of a low-molecular-weight, mucin-type glycoprotein from human submandibular-sublingual saliva. 713 59


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