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

A study was made of the association of actin with different plasma membrane fractions from liver of normal rats and from the enlarged liver of rats bearing a Walker 256 carcinoma where a decrease in the state of polymerisation of cytoplasmic actin has been previously observed. As estimated by the DNAase I inhibition assay, actin constituted approx. 7% and 3%, respectively, of the protein of membrane fractions enriched in lateral or bile-canalicular domains, but only trace amounts were found in the sinusoidal fraction. [3H]Cytochalasin B binding indicated the presence of 20 and 13 pmol of high-affinity binding sites per mg protein in lateral and bile-canalicular fractions, but none in the sinusoidal. Kd for cytochalasin B binding was of the order of 1 nM for lateral and bile-canalicular fractions. Polypeptide profiles obtained by SDS/urea/polyacrylamide gel electrophoresis of non-ionic detergent-insoluble residues differed for all three fractions although some proteins, including actin, occurred as major components of both bile-canalicular and lateral regions. Tumour growth had no effect on the actin content, high-affinity cytochalasin B binding or polypeptide profiles of the three membrane fractions.
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PMID:Plasma membrane associated actin in liver of normal and tumour-bearing rats. 405 15

Cytochrome c oxidase isolated from pig liver and heart was incubated with 1-ethyl-3-[3-(dimethyl-amino)propyl]carbodiimide and [14C]glycine ethyl ester in the presence and absence of cytochrome c. Labelling of individual subunits was determined after separation of the enzyme complexes into 13 polypeptides by SDS-gel electrophoresis. Polypeptide II and additional but different polypeptides were labelled in the liver and in the heart enzyme. Labelling of polypeptide II and of some other polypeptides could be partially or completely suppressed by cytochrome c. From the data two conclusions can be drawn: In addition to polypeptide II, other polypeptides take part in the binding of cytochrome c to cytochrome c oxidase; the binding domain for cytochrome c is different in pig liver and heart cytochrome c oxidase.
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PMID:Different reactivity of carboxylic groups of cytochrome c oxidase polypeptides from pig liver and heart. 608 6

Choroid plexus (GCP-3) cell cultures were prepared from an adult goat with symptoms of visna. The GCP-3 cell layer had partly fused into large multinucleated giant cells and electronmicrographs showed virus particles morphologically indistinguishable from sheep visna virus (SVV). A virus, designated goat visna virus (GVV), was subsequently purified from the GCP-3 cultures. The virus particles have a density of 1.15 g/ml and a high molecular weight RNA similar in size to that of SVV. A virion-associated DNA polymerase was identified which is stimulated to the same extent as the SVV polymerase by different synthetic RNA and DNA template-primer combinations and which shows the same Mg2+ and Mn2+ stimulation optima. Polypeptide analysis by SDS-PAGE revealed that the virion proteins of GVV and SVV had similar molecular weights. By immunodiffusion tests it was demonstrated that the major internal proteins of GVV and SVV are related. Consequently, we conclude that GVV should be classified as a retrovirus and that it is closely related to visna virus of sheep.
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PMID:Goat visna virus: isolation of a retrovirus related to visna virus of sheep. 616 82

Polypeptide and polysaccharide outer membrane components of Brucella abortus 99 (S) were investigated by analysis of cell-wall fractions by sodium dodecyl-sulfate polyacrylamide gel electrophoresis and staining with coomassie blue and periodic acid silver stain. Crude cell-walls were deprived by Triton X-100 treatment of most cytoplasmic material as seen by electron microscopy and cytochrome determination (cell-walls). They were submitted to hot SDS to obtain intentionally after centrifugation, peptidoglycan in the insoluble fraction: SDS-I fractions or peptidoglycan sacculi, and outer membrane components in the SDS soluble fraction as for Enterobacteriaceae. The SDS-soluble fraction contained two major components: a high molecular weight broad band of smooth lipopolysaccharide (S-LPS) and a 43k polypeptide band. The SDS-I fractions were treated by lysozyme to solubilize peptidoglycan before analysis. They contained two major polypeptide groups 36-37-38k, 25-26-27k, a minor one at 31k and variable amounts of high molecular weight S-LPS. The polypeptide and polysaccharide patterns of the entire outer membrane obtained from lysozyme hydrolysed cell-walls are the sum of both SDS soluble and insoluble fraction patterns. These results mean that 25-27k and 36-38k bands are strongly bound to peptidoglycan, probably covalently. The 25-26-27k bands heavily stained for polysaccharides would be glycopolypeptides. In addition, the polysaccharide patterns of S-LPS fraction appears as a high molecular weight broad band, contrary to the multiple regularly spaced bands of high molecular weight E. coli S-LPS. The B. abortus outer membrane is composed of four major components: LPS, 43k and 36-37-38k polypeptides and 25-26-27k glycopeptides.
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PMID:Evidence of three major polypeptide species and two major polysaccharide species in the Brucella outer membrane. 641 68

Six subcellular fractions were isolated by differential centrifugation of the homogenate of spermatozoa of Ascaris suum. The cellular constituents of pelleted fractions, as identified by electron microscopy, were membranes and membranous organelles (fraction A1), microsomal (A2), cytoplasmic (A3), large refringent granules (B1), small refringent granules (B2) and a detergent-soluble fraction (B3). Polypeptide analysis of SDS-PAGE showed that the 18,400-dalton band, one of the major spermatozoan proteins, is detectable in all of the fractions. However, the cytoplasmic (A1) and refringent-granule (B1) fractions contained the highest level. The isolated refringent granules consisted of 2-6% lipid while the nonlipid fraction formed an insoluble matrix with a fibrillar network morphology. This fibrillar matrix contained three polypeptides of small molecular weight (7,000-14,000) in addition to the 18,400-dalton polypeptide. These small polypeptides (7,000--14,000 MW) are detectable only in fractions of the refringent granules and are therefore called the refringent-granule proteins (RGP). These RGP are sensitive to tryptic hydrolysis and have solubility properties similar to the protein, ascaridine.
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PMID:Subcellular fractions and the refringent granules of the spermatozoa of Ascaris suum (Nematoda). 731 39

In vitro synthesis of proteins and changes in polypeptide composition of sarcolemma were studied in innervated and denervated extensor digitorum longus muscle of the rat. A technique of evacuating myoplasm from muscle slices was used as a preliminary step in the preparation of three membrane fractions, M, H and S, containing sarcolemma. On the basis of findings from the previous study and the present investigation, it was concluded that the M fraction was most enriched with extrajunctional sarcolemma. In vitro incorporation of [3H]leucine into membrane proteins of the M fraction showed an apparent linear increase in the rate of protein synthesis from 1-10 days after denervation. The relative increase at 10 days was 137% greater than that of innervated controls. Fractions H and S showed a smaller relative increase. Polypeptide composition of M, H and S fractions based on SDS gel electrophoresis of innervated and denervated muscle, showed qualitative and quantitative changes. The most striking difference was a nominal 29 000 component in M that constituted a disproportionately large peak. Following 10 days of denervation the M fraction underwent significant compositional changes in its electrophoretic profile, the most dramatic of which was a large reduction in the proportion of the 19 000 component. The denervation-induced compositional change is discussed in light of known alterations in the chloride conductance of the muscle plasmalemma.
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PMID:Effects of denervation on the composition and synthesis of sarcolemmal proteins. 740 6

Hepatitis B e antigen (HBeAg) occurs in the serum of individuals infected with hepatitis B virus both free and in association with IgG. Utilizing a succession of steps involving salt precipitation, affinity chromatography, ion-exchange chromatography and isoelectrofocusing, we isolated free and IgG-bound forms of HBeAg from the sera of infected individuals with an overall gain in specific activity of 3000-fold and 540-fold, respectively. Polypeptide profiles of purified HBeAg preparations were studied by SDS-polyacrylamide gel electrophoresis in the presence of 2-mercaptoethanol. Both free and IgG-bound preparations revealed polypeptides with mol. wt. of 15500 (P15.5) and 16 500 (P16.5), and HBeAg activity was detected corresponding to their positions. The HBeAg polypeptides (P15.5/16.5) derived from sera were physicochemically different from the two polypeptides with HBeAg activity (P19 and P45) liberated from Dane particle cores by the conventional method involving incubation with Nonidet P40 and 2-mercaptoethanol. However, when core particles were prepared in the presence of a proteolytic enzyme, in addition to Nonidet P40 and 2-mercaptoethanol, they gave rise to HBeAg polypeptides with mol. wt. of 31000 (P31) and 15 500. Furthermore, P31 split into P15.5 when heated at 100 degrees C for 2 min. On the basis of these results, P15.5 may be assumed to be the essential polypeptide bearing HBeAg activity in the serum and also in Dane particles.
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PMID:Hepatitis B e antigen polypeptides isolated from sera of individuals infected with hepatitis B virus: comparison with HBeAg polypeptide derived from Dane particles. 744 Dec 14

An Indian isolate of infectious bursal disease virus, i.e. IBDV-P/AD/81, was analysed for immunogenic activity of its structural polypeptides. Virus was purified from infected bursal homogenate by sucrose density gradient centrifugation. It showed five different structural polypeptides of 75.8, 45, 40.7, 33.1 and 27 kDa molecular weights in sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Anti infectious bursal disease virus (IBDV) antibodies were tested using enzyme-linked immunosorbent assay (ELISA) and neutralization test (NT). Polypeptide 40.7 kDa (VP2) was known to have neutralizing epitopes. However, polyclonal anti VP2 failed to neutralize the virus. It was interpreted that VP2 had labile neutralizing epitopes which get altered confirmationally by SDS. Surprisingly, polyclonal anti 33.1 kDa (VP3) had mild neutralizing activity.
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PMID:Immunogenic activity of viral polypeptides of an Indian isolate of infectious bursal disease virus. 782 77

Polypeptide synthesis and morphogenesis of a group C rotavirus (AmC-1) adapted to a continuous swine testicular cell line was examined. SDS-PAGE analysis of 35S methionine labeled infected cell lysates revealed 9 viral polypeptides (122, 98, 79, 78, 43, 41, 35, 24, and 20 kD). Viral polypeptide synthesis appeared to be maximal at 7-10h post infection. Purified group C virus grown in the presence of trypsin was found to contain seven structural polypeptides (122, 98, 79, 53, 43, 41, and 30 kD) by protein blotting and five polypeptides (98, 79, 78, 43, and 41 kD) by immunoprecipitation with a hyperimmune rabbit antisera. Tunicamycin treatment, Concanavalin A binding, protein blotting, endo-H treatment and 2,6H-mannose labeling suggested that group C rotavirus contains one structural glycoprotein (41 kD) with a corresponding precursor mol. wt. of 37 kD and one not previously identified nonstructural glycoprotein (24 kD) with a corresponding precursor mol. wt. of < or = 20 kD. Electron microscopy of infected swine testicular cells revealed an assembly process for group C rotavirus similar to group A, with single-shelled particles budding through the rough endoplasmic reticulum with concomitant acquisition of a transient membrane.
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PMID:Biosynthesis and morphogenesis of group C rotavirus in swine testicular cells. 824 12

The cellulosome of Clostridium thermocellum JW20 consists of 14-26 different polypeptides as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The intact cellulosomes hydrolyzes crystalline cellulose in the presence of Ca2+ and thiols. This activity is inhibited by ethylenediaminetetraacetic acid (EDTA). Ca is incorporated into the cellulosome and tightly bound as demonstrated using 45Ca added to the growth medium. Upon incubation in 50 mM Tris (pH 7.5), 0.1 M NaCl, and 5 mM EDTA at 37 degrees C, Ca is released from the cellulosome, which disintegrates into polypeptides. The SDS-PAGE pattern of cellulosomal polypeptides is remarkably different after the EDTA treatment when compared to this pattern of untreated cellulosomes. Polypeptide bands corresponding to molecular masses of 160, 98, 76, 91, and 54 kDa disappear, and new bands of masses 150, 132, 91, 71, 57, and 46 kDa appear. N-terminal analyses of the 98, 76, 91, and 71 kDa polypeptides show that the 91 and 71 kDa polypeptides are truncated products of the 98 and 76 kDa polypeptides, respectively. The 76 and 71 kDa polypeptides correspond to CelS [Wang, W. K., Kruus K., & Wu, J. H. D. (1993) J. Bacteriol. 175, 1293-1302]. The 71 kDa polypeptide is formed from the 76 kDa polypeptide during the EDTA treatment, by a cleavage that occurs at asparagine residue 681. It involves the removal of 60 amino acid residues from the C-terminal end. All catalytic subunits so far characterized contain an asparagine residue corresponding to residue 681 of CelS. This residue is part of the conserved duplicated region found in catalytically active subunits, and it is postulated that several of these subunits also are truncated by the EDTA treatment. The polypeptides truncated by the EDTA treatment reduced Ca binding capacities compared to their native subunits, indicating a Ca-binding site within the conserved duplicated region. This region has been implicated in the binding of the catalytic peptides to the scaffolding polypeptide CipA, which is a structural protein of the cellulosome and has a strong affinity for calcium.
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PMID:Dissociation of the cellulosome of Clostridium thermocellum in the presence of ethylenediaminetetraacetic acid occurs with the formation of trucated polypeptides. 866 81


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