Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Chinese hamster ovary cells cultured in the presence of phenethyl alcohol exhibit obvious changes in cell surface galactose and galactosamine glycoproteins as determined by the galactose-oxidase[3H]borohydride technique and SDS gel electrophoresis. Cells pretreated with phenethyl alcohol (drug was removed before infection) were not as effective as hosts for vesicular stomatitis virus as untreated cultures. A minimum pretreatment time with 0.1% phenethyl alcohol of about 8 h was required before a reduction in virus growth was observed. It is proposed that phenethyl alcohol pretreatment as outlined in this report leads to a modification of the host cellular membrane resulting in the inhibition of virus replication.
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PMID:Pretreatment of hamster cells with phenethyl alcohol alters cell surface glycoproteins and inhibits vesicular stomatitis virus growth. 6 7

The heterophile antigen (Paul-Bunnell antigen, PBA) of infectious mononucleosis was isolated by extraction of an aqueous suspension of bovine erythrocyte stromata with chloroform-methanol (2:1). The upper aqueous layer contained gangliosides, PBA, and a high-molecular-weight glycoprotein. PBA and gangliosides were separated from the high-molecular-weight glycoprotein by extraction of lyophilized upper layer with chloroform-methanol solvents. Separation of PBA from gangliosides was carried out by chromatography on DEAE-cellulose with chloroform-methanol solvents. PBA appeared to be a minor glycoprotein component of the erythrocyte membrane and had both hydrophobic and hydrophilic properties. It was soluble in either organic or aqueous solvents. On SDS-polyacrylamide gel electrophoresis, it migrated as a single component that stained for protein with Coomassie blue, for carbohydrate with periodic acid-Schiff reagent, and for lipid with oil red 0; it had an apparent molecular weight of 26,000. It was composed of 62% protein with major amino acids; glutamic acid, proline, glycine, isoleucine, leucine, and threonine (158, 116, 98, 90, 85, and 82 residues per 1,000 residues, respectively). Carbohydrate content was 9.2% with major sugar constituents: sialic acid, galactosamine, and galactose. Serologic activity of PBA was destroyed by pronase but not by trypsin.
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PMID:Isolation and partial characterization of the heterophile antigen of infectious mononucleosis from bovine erythrocytes. 40 89

D-Galactosamine administration to rats (400 mg/kg) by intraperitoneal injection induced biochemical alterations in liver plasma membranes. Alterations were studied 4, 16 and 24 h after D-galactosamine injection. Plasma membrane 5'-mononucleotidase activity decreased to 40% of control values. Carbohydrate composition was significantly changed. After 24 h D-galactosamine administration, the diminution in plasma membrane sialic acids and hexoses reached 30% of control values. As detected by SDS-acrylamide gel electrophoresis, high molecular weight glycoproteins of D-galactosamine-treated plasma membranes were modified. Moreover, the incorporation of [35S]-sulfate into membrane glycoproteins decreased after D-galactosamine administration (40--60% of control). The present results show that biochemical alterations in rat liver plasma membranes appear soon after D-galactosamine injection. Marked changes are observed in cell surface glycoproteins, especially in sialoglycoproteins and sulfated glycoproteins.
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PMID:Changes in glycoproteins of liver plasma membranes from rats treated with D-galactosamine. 48 50

A glycoprotein was isolated from goat erythrocyte membranes by extraction with hot 75% ethanol. The glycoprotein was purified by ethanol precipitation, phosphocellulose chromatography gel filtration, ethyl:ether and chloroform:methanol extraction. In aqueous phosphate-buffered saline, pH 7, the glycoprotein was in an aggregated state with a sedimentation coefficient (S(obs)) to 1.5. Electrophoresis of the glycoprotein on polyacrylamide gels containing phosphate-buffered 0.1% SDS gave a single band, staining with both periodic acid Schiff (PAS) and Coomassie Blue (CB). The apparent m.w., calculated from retardation coefficient, was 25,000. Electrophoresis of the glycoprotein on 1% SDS gels buffered with Tris-acetate (pH 7.4) showed a major band of similar (23,500) apparent m.w. plus four other PAS- and CB-staining bands of lower mobility. With 131I-labeled glycoprotein, recovery of bands from gels, sialic acid analysis, heterophile antigen activity, and re-electrophoresis, it was shown that these additional bands were aggregated forms of a single or closely related glycoprotein species. The purified glycoprotein contained 50% carbohydrate with molar ratios of sialic acid:galactose:mannose:galactosamine:glucosamine of 3.1:2.1:0.1:1.6:1. The glycoprotein was highly reactive with the Paul-Bunnell heterophile antibody in the sera of patients with infectious mononucleosis, with Limulus polyphemus lectin and weakly ractive with wheat germ agglutinin. These reactivities were destroyed by neuraminidase treatment or by alkaline sodium borohydride. The native glycoprotein did not react with lectins from Canavalia enisformis, Phaseolus vulgaris, Ricinus communis, or Vicia graminea although it was reactive with the latter two after neuraminidase treatment.
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PMID:Immunochemical studies of infectious mononucleosis. V. Isolation and characterization of a glycoprotein from goat erythrocyte membranes. 95 50

1. Brush border membrane vesicles (BBMV) were prepared from the Bombyx mori, and Spodoptera litura, midguts. BBMV was solubilized. 2. Activated delta endotoxin from Bacillus thuringiensis were immobilized. 3. Solubilized BBMV proteins were applied to the toxin column and the proteins bound were analyzed by SDS-PAGE. 4. In the case of B. mori M(r) = 220,000, 150,000 and 130,000 and in the case of S. litura 160,000 bands were detected. 5. The bindings were inhibited by N-acetyl galactosamine and mannose. 6. The binding proteins applied onto a Con A column and eluted by 0.1 M methyl-alpha-glucose, suggesting that hybrid type sugar sidechain may involve in the interaction.
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PMID:Isolation and partial characterization of binding proteins for immobilized delta endotoxin from solubilized brush border membrane vesicles of the silkworm, Bombyx mori, and the common cutworm, Spodoptera litura. 132 44

The specific binding and nature of the epitope recognized by monoclonal antibody (Mab) 1H10, which binds an antigen expressed on human cervical tumors, was characterized by enzyme digestion, lectin competition assay and immuno-electron microscopy. Membrane homogenates of CaSki cervical carcinoma cells were digested with various enzymes, then analysed by SDS-PAGE and immunoblotting. Cells grown on coverslips were treated with various enzymes and in situ binding of Mab 1H10 to cells was analysed by electron microscopy. The ability of lectin-conjugates to block Mab 1H10 binding to CaSki cells was also examined. Treatment of samples with sodium periodate abrogated antigen recognition by Mab 1H10. Neuraminidase and hyaluronidase digestion decreased but did not eliminate Mab 1H10 binding to cells in situ. Chondroitinase ABC digestion, in contrast, removed Mab 1H10 binding sites both in vitro and in situ. Trypsin and chymotrypsin digestion of cell membrane homogenates decreased the molecular weight of the Mab 1H10 antigen but did not decrease the binding intensity. Wheat germ agglutinin (WGA) strongly bound to CaSki cells and partially blocked Mab 1H10 binding, indicating that the antigen contains N-acetyl-galactosamine residues at or near the epitope recognized by Mab 1H10. Ricinus communis agglutinin (RCA) exhibited a similar binding pattern to WGA. However, concanavalin A bound only weakly to CaSki cells and was ineffective at blocking Mab 1H10 binding. The tumor-associated antigen recognized by Mab 1H10 is concluded to be a chondroitin sulphate glycoprotein or proteoglycan rather than a mucopolysaccharide or lipoprotein.
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PMID:Characterization of a human cervical carcinoma-associated antigen by lectin binding and immuno-electron microscopy. 142 5

A chitobiase gene from Vibrio parahemolyticus was cloned into plasmid pUC18 in Escherichia coli strain DH5 alpha. The plasmid construct, pC120, contained a 6.4 kb Vibrio DNA insert. The recombinant gene expressed chitobiase [EC 3.2.1.30] activity similar to that found in the native Vibrio. The enzyme was purified by ion exchange, hydroxylapatite and gel permeation chromatographies, and exhibited an apparent molecular weight of 80 kDa on SDS-polyacrylamide gel electrophoresis. Chitobiose and 6 more substrates, including beta-N-acetyl galactosamine glycosides, were hydrolyzed by the recombinant chitobiase, indicating its putative classification as an hexosaminidase [EC 3.2.1.52]. The enzyme was resistant to denaturation by 2 M NaCl, thermostable at 45 degrees C and active over a very unusual (for glycosyl hydrolases) pH range, from 4 to 10. The purified cloned chitobiase gave 4 closely focussed bands on an isoelectric focusing gel, at pH 4 to 6.5. The N-terminal 43 amino acid sequence shows no homology with other proteins in commercial databanks or in the literature, and from its N-terminal sequence, appears to be a novel protein, unrelated in sequence to chitobiases from other Vibrios reported and unrelated to hexosaminidases from other organisms.
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PMID:Thermostable, salt tolerant, wide pH range novel chitobiase from Vibrio parahemolyticus: isolation, characterization, molecular cloning, and expression. 142 6

Sialoglycoprotein with a molecular mass of 85 kDa (LGP85) was purified from rat liver lysosomal membranes with a 0.9% recovery to apparent homogeneity, as determined from the pattern on polyacrylamide gel electrophoresis in the presence and in the absence of SDS. The purification procedures included: preparation of lysosomal membranes, elimination of LGP107 and LGP96 with immunoaffinity columns, WGA-Sepharose affinity chromatography, hydroxylapatite chromatography, and preparative polyacrylamide gel electrophoresis. LGP85 contains about 22.8% carbohydrate and the carbohydrate moiety is composed of mannose, galactose, fucose, glucosamine, galactosamine, and neuraminic acid, in a molar ratio of 40:20:2:23:3:13. Susceptibility to neuraminidase and immunoreactivity of the protein in intact tritosomes were examined to study the topology of the protein in tritosomal membranes. Neuraminidase susceptibility and immunoreactivity of the protein were not observed in intact tritosomes until the tritosomes had been disrupted by osmotic shock. These observations suggest that both oligosaccharide chains and the main protein portion of the protein are located on the interior surface of the tritosomal membranes. Subcellular localization of LGP85 was determined using enzyme immunoassay. The lysosomes seem to be the major location. LGP85 in the lysosomes was divided into the membrane bound form (90%) and the soluble form (10%). Immunoelectron microscopy clearly confirmed that the localization of LGP85 is mainly confined to lysosomes.
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PMID:Purification and characterization of an 85 kDa sialoglycoprotein in rat liver lysosomal membranes. 150 Apr 17

The presence of membrane-associated proteins which stereospecifically bind cyclosporin A and react with anti-cyclophilin antibodies has been documented in rat tissues. Extraction of membranes with 6 M urea or 0.5% Chaps releases cyclosporin-binding activity that is 5-12% of that found in cytosol. Cyclosporin-A-binding proteins are present in most subcellular organelles of liver, but microsomes contain the greatest activity. These proteins can be purified by adsorption onto a cyclosporin-A affinity column and elution with cyclosporin A. Two major fractions are resolved on SDS/PAGE: an 18-kDa fraction is comprised of two isoforms that are similar if not identical to the two major cytosolic isoforms of cyclophilin. In addition, in microsomes an approximately equal quantity of a 22-kDa glycoprotein was detected. Based on partial sequencing (five peptides, 89 amino acids) this protein is similar but not identical to human cyclophilin B. This 22-kDa isoform is poorly recognized by affinity-purified anti-cyclophilin antibodies and comprises several predominant isoforms (pI approximately 9.3-9.6). Selective binding of membrane 22-kDa cyclophilin to peanut lectin suggests the oligosaccharides contain a terminal galactosyl-N-galactosamine residue.
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PMID:Isolation and partial characterization of membrane-associated cyclophilin and a related 22-kDa glycoprotein. 158 81

Two major glycoproteins (PAS-6 and PAS-7) from bovine milk fat globule membrane were selectively extracted with urea and KCl, co-purified by repeated gel filtration on Sephacryl S-200 and then separated by affinity chromatography on concanavalin A-agarose column. The two purified glycoproteins showed a single band by SDS-PAGE, and their molecular masses were estimated to be 50 kDa for PAS-6 and 47 kDa for PAS-7. Both PAS-6 and PAS-7 were resolved several variants by analytical isoelectric focusing. These were shifted to a single band at pI 6.2 for PAS-6 and at pI 6.5 for PAS-7 by neuraminidase. PAS-6 contained 7.1% and PAS-7 5.5% of carbohydrate; the molar ratio of fucose:mannose:galactose:N-acetyl galactosamine:N-acetyl glucosamine:sialic acid was 1.0:3.0:2.0:6.1:5.0:1.3 for PAS-6 and 1.0:3.1:2.2:0:4.1:1.1 for PAS-7. Mild alkaline treatment and affinity to various lectins indicated that PAS-6 had O- and N-linked oligosaccharide chains, while PAS-7 had only the N-linked type. The major amino acid residues of PAS-6 were Glu, Ser and Gly, and those of PAS-7 were Asp, Glu, Gly and Leu. The N-terminal amino acids of both glycoproteins were blocked. PAS-6 and PAS-7 digested with trypsin had a different peptide map, two major peptides having the same retention time on HPLC and being common to PAS-6 and PAS-7 having the same amino acid sequences of H-Gln-Ser-Gly-Asn-Lys-Asn-Pro-Ser-Glu-Ile-Ser-OH and H-Ile-Phe-Pro-Gly-Asn-Met-Asp-Asn-Ser-His-Lys-OH.
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PMID:Purification and characterization of major glycoproteins, PAS-6 and PAS-7, from bovine milk fat globule membrane. 164 94


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