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)

Neither normal nor hemophilic factor VIII protein enters a 5% sosium dodecyl sulfate gel; on reduction, however, a single 195 000-molecular-weight peptide is observed. Hemophilic and normal factor VIII contain carbohydrate and appear identical in subunit molecular weight, electrical charge, and major antigenic determinants. Thrombin activation and inactivation of factor VIII does not detectably change the subunit molecular weight. Trypsin causes similar activity changes and obviously cleaves the factor VIII subunit. Human plasmin destroys factor VIII procoagulant activity and degrades the factor VIII subunit to 103 000-, 88 000-, and 17 000-molecular-weight peptides. Both normal and hemophilic factor VIII as well as thrombin-inactivated factor VIII support ristocetin-induced platelet aggregation. Purified factor VIII chromatographed on 4% agarose in 1.0 M sodium chloride shows no dissociation of the procoagulant activity from the void volume protein. Gel chromatography on 4% agarose in 0.25 M calcium chloride results in a procoagulant activity peak removed from the void volume protein; both peaks contain protein which does not enter a 5% SDS gel, but on reduction a 195 000-molecular-weight subunit band is observed for each. Both the void volume protein peak and the procoagulant activity peak from the 0.25 M calcium chloride-agarose gel column support ristocetin-induced platelet aggregation. After removal of calcium, a small amount of procoagulant activity is present only in the void volume peak. These data suggest that both the procoagulant and von Willebrand activities are on the same molecule. Thus our previous conclusion remains the same: human factor VIII is a large glycoprotein composed of identical 195 000-molecular-weight subunits jointed by disulfide bonds and is responsible for both antihemophilic and von Willebrand activities in human plasma.
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PMID:Molecular structural studies of human factor VIII. 12 89

Proteins are important constituents of the red blood cell plasma membrane. Several important breakthroughs have occurred in their analysis over the past few years. SDS-polyacrylamide gel electrophoresis lead to the separation of the major proteins and glycoproteins. Location of most of these proteins -- either on the external, the internal or both surfaces of the membrane -- was determined. The strenght of the binding of the protein to the membrane was established. Hydrophobicity of membrane proteins has so far hindered their purification. However, the major glycoprotein (glycophorin A) was isolated and recently sequenced. The description of several membrane-associated enzyme activities has been followed by some understanding of their specific role in the red blood cell physiology. Abnormalities of glycoproteins, Ca2+-ATPase and of membrane protein phosphorylation have been reported under various conditions: sickle cell disease, hereditary spherocytoses, progressive muscular dystrophy.
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PMID:[Erythrocyte membrane proteins]. 14 51

Membrane-bound and free polyribosomes were isolated from skeletal muscle of neonatal rats and messages were translated in a rabbit reticulocyte lysate treated with Ca2+ -dependent nuclease to reduce endogenous messenger translation. Newly synthesized calsequestrin and adenosine triphosphatase (ATPase) sere isolated by antibody precipitation, followed by separation of the precipitates in SDS-polyacrylamide gels. Radioactivity in calsequestrin and the ATPase were counted in gel slices. Calsewuestrin and the ATPase were both found to be synthesized on membrane-bound polyribosomes. Since calsequestrin is a glycoprotein, localized in Golgi regions in early stages of muscle cell differentiation, it is probable that its synthesis follows the pathway for synthesis of secreted proteins except that its destination is the luminal space of a cellular organelle. The disposition of the ATPase during synthesis is, as yet, unknown.
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PMID:Assembly of the sarcoplasmic reticulum. Synthesis of calsequestrin and the Ca2+ + Mg2+ -adenosine triphosphatase on membrane-bound polyribosomes. 14 86

Acetylcholinesterase from Banded krait (Bungarus multicinctus) venom has been purified by CM-Sephadex chromatography and affinity chromatography to a specific activity of 4290 U/mg. The purified enzyme is a glycoprotein. It is free of electrophoretically detectable contaminating proteins. A molecular weight of 140,000 +/- 5,000 has been determined by gradient gel electrophoresis for the native enzyme. It is split into two equal-sized subunits (Mr 70,000 +/- 2,000) by SDS treatment. The N-terminal amino acid analysis gave glycine and serine. The purified acetylcholinesterase can be resolved by disc gel electrophoresis into four and by isoelectric focusing into six isozymes. The pI value of the main isozyme has been found to be 5.98 +/- 0.05.
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PMID:[The acetylcholinesterase of Bungarus multicinctus venom. Purification and properties (author's transl)]. 15 47

Acetylcholinesterase was released from bovine erythrocytes by Triton X-100 treatment and purified by twwfold affinity chromatography. The detergentfree enzyme was obtained with a specific activity of 4130 U/mg (303 000-fold purification) and a 25% yield. Alternatively, the commercial available crude enzyme was purified. The latter preparation has an uniform molecular weight (Mr 175 000). The Triton-solubilized enzyme, however, can be resolved after removal of the detergent in eight multiple forms (Mr 175 000 and multiple values), in the presence of Triton there exists only one form (Mr 338 000). The amino acid composition of the two enzyme preparations differs significantly. No differences were observed with respect to other properties: SDS gel electrophoresis revealed two protein bands (Mr 166 000 and 86 000) with both preparations. The enzyme is a glycoprotein with a pI value of 4.3 and contains strongly bound phosphatidylethanolamine. The N-terminal amino acid has been found to be Glu (or Gln).
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PMID:[Acetylcholinesterase from bovine erythrocytes. Purification and properties of the enzyme solubilized in the presence and the absence of Triton X-100 (author's transl)]. 16 Jun 95

Direct immunodiffusion comparison with specific antisera demonstrated that all of the four pregnancy-associated plasma proteins (PAPPs) described in our laboratory are distinct from the pregnancy zone protein (von Schoultz); alpha2-pregnoglobulin (Berne); pregnancy-associated alpha2-glycoprotein (SP3) (Bohn); new serum alpha2-macroglobulin (Stimson); PAG (Horne); pregnancy-associated alpha2-globulin (Kasukawa); Pal (McLaren), and Xh protein (Dunston). All the latter proved to be immunologically idnetical to each other, and apparently represent the same protein described under different names. It was confirmed that none of the PAPPs is immunochemically related to placental alkaline phosphatase. PAPP-A, PAPP-C, and the pregnancy zone protein, but not HPL (PAPP-D), showed a decreased anodic mobility when treated with neuraminidase; their reactivities with antibody were essentially unaffected by the ezyme, however. Certain detergents had no effect on the immunological reactivities of the PAPPs and the pregnancy zone protein in whole plasma, while butanol and desoxycholate partially, and urea, SDS and cetylpyridinium largely inactivated them.
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PMID:Immunological comparison of various human pregnancy-associated plasma proteins. 16 2

The protein and glycoprotein composition of Kirsten murine leukaemia-sarcoma virus (KiMSV(KiMuLV) was studied using SDS-polyacrylamide gel electrophoresis. Twenty-three polypeptides and three glycoproteins were detected following electrophoresis by staining with Coomassie blue and PAS or by autoradiography of isotopically labelled virus. Protein components were assigned positions in the virus particle, envelope, nucleoid or intermediate area based on iodination with lactoperoxidase and sedimentation in potassium citrate equilibrium gradients. The KiMSV (KiMuLV) envelope contained 11 polypeptides and three glycoproteins. The virus nucleoid and intermediate area were each composed of six proteins. The protein composition of KiMSV(KiMuLV) was highly reproducible when virus was harvested from cells of the same subcluture generation. However, the protein profiles were altered with repeated in vitro passages of the virus-producing cell line.
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PMID:Proteins of Kirsten murine leukaemia-sarcoma virus: localization within the virus particle by iodination and fractionation techniques. 16 14

Egg-grown Sendai virus was used for preparation of rabbit hyperimmune sera directed against purified whole virus and pronasetreated projectionless virus particles. These sera and convalescent sera after natural Sendai infection in guinea pigs were studied in haemolysis-inhibition (HLI), haemagglutination-inhibition (HI) and neuraminidase-inhibition (NI) tests both before and after absorption with Tween 80-ether (TE) treated virus preparations. In addition, neutralization tests using the different sera were carried out. HI and NI antibodies and the major population of neutralizing antibodies in convalescent sera were removed by absorption with TE treated virus material without changing the titre of non-HI HLI antibodies. Rabbit hyperimmune sera directed against projectionless virus particles exhibited HLI antibody titres in marked excess of HI and NI antibody titres, whereas this was not found in sera against purified whole virus. In contrast, absorption of sera against projectionless particles eliminated HI antibodies without changing the titre of non-HI HLI antibodies. The protein composition of antigenic preparations used in absorption experiments and for preparation of sera was investigated by SDS-polyacryladmie-gel electrophoresis. TH treatment had no significant effect on the polypeptide pattern of Sendai virus. Pronase-treatment predominantly affected the two glycosylated proteins of Sendai virus. The larger glycoprotein was not detectable in pronasetreated projectionless virus particles, whereas the smaller glycoprotein was present in reduced quantities.
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PMID:Identification of paramyxovirus-specific haemolysis-inhibiting antibodies separate from haemagglutinating-inhibiting and neuraminidase-inhibiting antibodies. 1. Sendai virus haemolysis-inhibiting antibodies. 18 12

A low molecular weight angiotensin I converting enzyme (light angiotensin enzyme) was isolated from a homogenate of rat lung subjected to dialysis against sodium acetate at pH 4.8. This enzyme has a molecular weight of 84 000 on Sephadex G-200 and a molecular weight of 91 000 on SDS-poly-acrylamide gel as compared with a molecular weight of 139 000 for angiotensin I converting enzyme on SDS-polyacrylamide. Light angiotensin enzyme was activated by NaCl and inhibited by EDTA, angiotensin II, and bradykinin potentiating factor nonapeptide. Light angiotensin enzyme cross-reacted with antibody prepared against angiotensin I converting enzyme and stained with periodic acid-Schiff reagent as a glycoprotein. The evidence suggests that light angiotensin enzyme is a fragment of the higher molecular weight enzyme.
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PMID:Low molecular weight angiotensin I converting enzyme from rat lung. 19 Oct 87

The proteins of visna are separated into nine major peaks by agarose gel chromatography in 6 M guanidine hydrochloride (GuHCl). The polypeptides in eack peak were isolated by acid precipitation and analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The patterns of SDS-PAGE show that the excluded material from the GuHCl column contains an aggregate of 10 non-glycosylated polypeptides. It is shown that this aggregate represents virus substructures that are not completely solubilized by GuHCl. Two glycoproteins, gp175 and gp115, were isolated from the column eluate. The major glycoprotein gp115 was coeluted with P90, P68, and P61 in GuHCl 4. Each of the four major peaks (GuHCl 5 to 8) contains more than one nonglycosylated polypeptide. However, a small polypeptide, P12, can be isolated in a homogeneous form in the last peak, GuHCl 9. Analysis of the virus proteins (100 microgram) by SDS-PAGE shows that 20 radioactive bands can be recognized. During fractionation of the protein on agarose gel columns followed by analysis with SDS-PAGE, a number of minor polypeptides that were not detected before became clearly recognizable. Thus, the combined use of column chromatography and SDS-PAGE shows that visna virus is composed of 25 proteins.
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PMID:Polyacrylamide gel electrophoresis of visna virus polypeptides isolated by agarose gel chromatography. 20 37


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