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

A method has been established which isolated polysomes from the lysozyme/EDTA-shocked cyanobacterium, Nostoc sp. MAC. In a typical preparation the total recovery of RNA as polysomes was 83%, in which 77% of the polysome fraction was present at sizes greater than 5-mers and 23% as 2-4-mers. Messenger RNA isolated from such a preparation of polysomes produced a 10-fold stimulation in the incorporation of [35S]methionine into polypeptides by a cell-free system of Escherichia coli. The in vitro-synthesized polypeptides were analysed on an SDS-polyacrylamide gradient gel together with in vivo-labelled proteins of Nostoc sp. MAC: seven polypeptides co-migrated with the in vivo-synthesized products. This is the first report of the expression of cyanobacterial messenger RNA in a heterologous cell-free system from E. coli; the efficiency of the system is discussed.
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PMID:Isolation of polysomes from Nostoc sp. MAC and translation of messenger RNA in a heterologous cell-free system. 641 28

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

Natural and synthetic antioxidants have been shown to repair tryptophan radicals produced from the one-electron oxidation of the free tryptophan amino acid. It has also been observed that both tryptophan and tyrosine radicals in lysozyme can be repaired by these antioxidants to varying degrees of efficiency. Although SDS-solubilized alpha-tocopherol efficiently repairs free tryptophan radicals, it is very inefficient in repairing the amino acids in lysozyme. The rigidity and immobility of solubilized alpha-tocopherol can explain this lack of efficiency.
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PMID:The repair of oxidized amino acids by antioxidants. 650 64

The occurrence of post-exercise proteinuria was investigated in intact and splenectomized dogs after treadmill running and swimming and compared to control experiments. Albumin and lysozyme were measured by radial diffusion. Urinary protein was analyzed by SDS-polyacrylamide gel electrophoresis. Swimming in the splenectomized dogs increased the albumin excretion in the first 30 min after exercise from 0.03 to 0.22 mg X min-1 and the lysozyme excretion in the same period from 0.11 to 0.75 micrograms X min-1. Swimming in intact dogs caused smaller increase in the lysozyme and albumin excretions during the exercise period itself as well as in the albumin excretion in the first 30 min after exercise. Running had no effect on urinary albumin or lysozyme but increased the low molecular weight protein fraction in the splenectomized dogs. Plasma lactate concentrations were higher during swimming in the splenectomized dogs than in the intact dogs. Possible mechanisms of post-exercise proteinuria are discussed.
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PMID:Proteinuria in intact and splenectomized dogs after running and swimming. 651 Nov 48

Protein A (PA)-activity was detected in Staphylococcus aureus strain Wood 46 which had been considered to be PA-negative. This staphylococcal strain bound 28% of 125I-labelled IgG, compared with 89% by strain Cowan I. The binding activities of both S. aureus strains were saturable, time-dependent and specific. The dissociation constants of 1.6 X 10(-9) M for Wood 46 and 9.3 X 10(-8) M for Cowan I indicated a similar affinity for human IgG in both strains. The number of IgG-binding sites were estimated to be 16,970 for Wood 46 and 41,200 for Cowan I. Exposure to heat and ultrasonication reduced PA-activities of strain Cowan I, but not that of strain Wood 46. Extraction of the staphylococci with guanidine and formic acid resulted in a reduction of IgG-binding activities only in strain Wood 46. Photooxidation, trypsinization and lysozyme treatment also diminished IgG-binding of strain Wood 46 to a larger extent than that of strain Cowan I. Extracellular PA from S. aureus strains Wood 46 and Cowan I could be purified by affinity chromatography on IgG-sepharose. The purified PA preparations gave single protein bands upon SDS-polyacrylamide gel electrophoresis. Their molecular weights were 42,000 and their isoelectric points approximated 5.0.
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PMID:Characterization of immunoglobulin G binding to Staphylococcus aureus strain Wood 46. 653 38

Using strains of Streptococcus mutans suspended in human saliva, the salivary proteins capable of binding to the surface of the bacteria were identified by immunological and electrophoretic techniques. Six binding components were recognized: IgA, lysozyme, some high molecular weight material (greater than 400,000), probably a glycoprotein, a low molecular weight component (11-13,000), a 150,000 mol. wt protein, and one major component, mol. wt 20-25,000 which did not resolve fully on SDS-polyacrylamide electrophoresis. All these salivary components could be desorbed from the bacteria with 1 M NaCl, and subsequent extraction of the same cells with 6 M guanidine-HCl did not release any more salivary material. The significance of the binding of these salivary components is unknown but some may modify the behaviour of the organisms in vivo.
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PMID:The adsorption of human salivary components to strains of the bacterium Streptococcus mutans. 659 86

The outer membrane of Vibrio parahaemolyticus strain 3283-61 (serotype O2:K3) was isolated from blebs released upon spheroplast formation, in the presence of lysozyme and EDTA, by isopycnic sucrose density gradient centrifugation. SDS-PAGE of the outer membrane fraction prepared from cells grown in nutrient broth containing 3% (w/v) NaCl revealed five major proteins, designated a to e, with apparent approximate molecular weights: a, 44 000; b, 36 000; c, 33 500; d, 26 500; e, 22 000. An increase in NaCl concentration in the growth medium resulted in an increase of proteins b and c, whereas a decrease to 0.5% (w/v) induced two additional major proteins with respective molecular weights of about 35 000 and 32 000. Proteins a and b appeared to be loosely associated with the peptidoglycan layer since they were largely retained after extraction with 2% (w/v) SDS at 50 degrees C for 30 min. Proteins c and/or e may play a role in phage VP1-receptors since phage-resistant mutants derived from strain 3283-61 had significantly diminished amounts of both proteins. The major outer membrane proteins varied in number and molecular weight in strains of V. parahaemolyticus belonging to different K-serotypes.
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PMID:Isolation and characterization of the outer membrane from Vibrio parahaemolyticus. 665 59

Circular dichroism measurements revealed that hen egg-white lysozyme underwent multiple conformational transitions upon the addition of acetic acid. The transitions were reversible as judged from complete recoveries of enzymatic activity, electrophoretic mobility in SDS-polyacrylamide gel, and of ellipticity. Two transitions, with the mid-concentrations of 26 and 38% (v/v), were observed with the CD spectra in the amide absorption region. The two transitions were essentially athermal in the temperature ranges, 0 to 25 degrees C for the former and -10 to 10 degrees C for the latter. The trough ellipticity for the product of the transition at the higher acetic acid concentration (DII form) very closely approached the value for the synthetic polypeptides in the beta-conformation as the temperature was lowered. Molecular weight measurements by sedimentation equilibrium indicated that the products were both monomeric. Measurements of CD spectra in the aromatic absorption region showed another transition, whose mid-concentration varied with temperature from 26% (v/v) (at about 25 degrees C) to 38% (v/v) (at -10 degrees C). A change in the hydrodynamic volume detectable by exclusion chromatography was associated with this transition only.
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PMID:Multiple conformational transitions of hen egg-white lysozyme in aqueous acetic acid solutions. 669 90

The spore-coat fraction from Bacillus megaterium KM, when prepared by extraction of lysozyme-digested integuments with SDS (sodium dodecyl sulphate) and urea, contains three N-terminal residues and a major component of apparent mol.wt. 17500. Electron microscopy of this fraction shows it to consist of an ordered multilamellar structure similar to that which forms the coat region of intact spores. The 17500-dalton protein, which has been purified to homogeneity, has an N-terminal methionine residue, has high contents of glycine, proline, cysteine and acidic amino acids and readily polymerized even in the presence of thiol-reducing agents. It is first synthesized between late Stage IV and early Stage V, which correlates with the morphological appearance of spore coat. Before Stage VI the 17500-dalton protein is extractable from sporangia by SDS in the absence of thiol-reducing reagents. Between Stage VI and release of mature spores the protein becomes resistant to extraction by SDS unless it is supplemented by a thiol-reducing reagent. In addition to that of the spore-coat protein, the timing of synthesis of all the integument proteins was analysed by SDS/polyacrylamide-gel electrophoresis and non-equilibrium pH-gradient electrophoresis. Several integument proteins are conservatively synthesized from as early as 1h after the end of exponential growth (t1), which may reflect protein incorporation into the spore outer membrane.
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PMID:Characterization, purification and synthesis of spore-coat protein in Bacillus megaterium KM. 680 68

Attempts at isolating individual human milk proteins showed that cross interactions made it difficult to obtain of homogeneous components. A new method was devised, based on complete precipitation of milk proteins with saturated ammonium sulphate and progressive solubilization of the precipitate on a column of Sephadex G10 with a linear gradient of ammonium sulphate (from saturation to water). Three fractions were obtained. The first contained lactoferrin, serum albumin, lysozyme and traces of alpha-lactalbumin. Lysozyme could be obtained free from contaminants by chromatography on Ultrogel AcA 54. Lactoferrin and serum albumin coeluting as a single peak, were separated by a further chromatography on DEAE-cellulose. From the other two fractions recovered on Sephadex G10, it should be possible to prepare immunoglobulins, alpha-lactalbumin and the bulk of caseins. The homogeneity of the preparations of lysozyme, lactoferrin and serum albumin was assessed by SDS polyacrylamide gel electrophoresis, acrylamide agarose electrophoresis and immunoelectrophoresis.
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PMID:[A new method for human milk protein separation]. 682 Nov 60


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