Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P30536 (PBS)
 9,886 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Several mucolytic agents were evaluated on sputum for testing their viscolytic activity and the bacterial tollerance to each of them. Proteolytic enzymes (trypsin, pepsin, papain, pancreatin), KJ, and dithiothreitol (or its derivatives) were better tollerated by common respiratory pathogens (H. influenzae, D. pneumoniae, Klebsiella, etc.) than other mucolytic agents, as acetil-cysteine, cisteamine-HCl, tension active substances, mercaptoethanol, and others. The dithiothreitol showed also one of the strongest viscolytic effect and therefore it was selected for the routinary sputum digestion at the concentration 0.1% in PBS pH 7.2. Such a solution was added to sputum specimen in different proportions according to the macroscopic "apparent" viscosity of each specimen. However researches on the comparative viscolytic activity of all the agents hereinafter considered are still in progress.
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PMID:[Study on the viscolytic activity of the sputum (author's transl)]. 1 42

A small endodeoxyribonuclease )2.3 S) that is active on single-stranded DNA has been extensively purified from Escherichia coli so as to be free of other known DNases. It has an alkaline pH optimum (9.5), requires Mg2+, and makes 3'-hydroxy and 5'-phosphate termini. The nuclease nicks duplex DNA, particularly if treated with OsO4, irradiated with ultraviolet light, or exposed to pH 5. The uracil-containing duplex DNA from the Bacillus subtilis phage PBS-2 is an especially good substrate; it is made acid-soluble by levels of the enzyme which fail to produce any acid-soluble material in other single-stranded or duplex DNAs. Neither RNA nor RNA-DNA hybrid are degraded by the enzyme. The enzyme specificity suggests that it might act at abnormal regions in DNA, so that its in vivo function could be to initiate an excision repair sequence. Its high activity on uracil-containing DNA could imply that the enzyme provides an alternative mechanism for excising uracil residues from DNA to the pathway utilizing uracil-DNA N-glycosidase. We suggest that this enzyme be designated as endonuclease V of E. coli.
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PMID:Endonuclease V of Escherichia coli. 1 59

Induction of a celayed-type hypersensitivity reaction in tuberculin-sensitized animals by tuberculin purified protein derivative (PPD) at the site of dermal vaccinia virus (VV) infection markedly accelerated elimination of VV and led to clinical recovery. Viral titers were depressed by over 99.9% in the skin of animals given PPD as compared to animals given phosphate-buffered saline or nonspecific irritants. Low concentrations of acid labile interferon were found in the skin of uninfected tuberculin-sensitized animals challenged with PPD. High concentrations of acid stable interferon were found in skin of tuberculin-sensitized animals infected with VV and challenged with either PPD or PBS. The time of appearance of the acid stable interferon was markedly accelerated, however, in the animals challenged with PPD as compared with PBS. It is concluded that recovery from dermal vaccinia infection can be enhanced by induction of a local delayed-type hypersensitivity reaction with an antigen untelated to the infecting virus.
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PMID:Inhibition of vaccinia virus replication in skin of tuberculin-sensitized animals challenged with PPD. 6 89

The volume of human red blood cells (RBC) was evaluated by means of the centrifugation method (hematocrit) and 131-J-labelled human serum albumin, respectively. Both of the methods yielded an identical volume of about 107 micron3 of the single RBC, provided the evaluation was performed in autologous plasma. Contrary to the 131-J-albumin method the results of which were found independent of various pretreatments of RBC, the centrifugation hematocrits of RBC previously washed with PBS and resuspended in PBS or saline protein media resulted in a mean cell volume of about 86 micron3. The decrease of the cell volume was associated with an efflux of K+ ions. If the RBC are centrifuged at 800 g instead of 15000 g, their volume will remain unchanged. The assessment of cytodeformability has shown, that RBC in PBS by loss of cell volume could enter a 2.3 micron micropipette completely. RBC in plasma, though traversing a 2.9 micron micropipette were incapable of entering a 2.3 micron channel completely. With pressures ranging from 300 to 350 mm H2O the processes of these cells undergo microspherulation.
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PMID:[Environmentally dependent erythrocyte membrane permeability as a source of error in the determination of hematocrit]. 7 10

LAL would not form a clot when mixed with a viscous, opaque parenteral preparation of iron dextran spiked with endotoxin. However, recoverable precipitate could be obtained by diluting the LAL iron dextran mixture with PBS and centrifuging. Although the pellet so formed was red colored the protein present could be quantitated by dissolving it in a Coomassie Blue stain solution. The very rapid change in color from reddish black to deep blue was measured quantitatively in a spectrophotometer and was sigmoidally related to the amount of endotoxin used to spike the iron dextran. This method is suggested to be generally useful to measure quantitatively endotoxin concentrations too low to form a clot with LAL but high enough to precipitate recoverable protein from LAL.
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PMID:Endotoxin determination in viscous opaque solutions of iron dextran by Limulus amebocyte lysate. 9 34

The contractile sheaths of five defective, PBS X-like bacteriophages from Bacillus subtilis and B. licheniformis were investigated by electron microscopy, dodecylsulphate gel electrophoresis and immunodiffusion. Electron microscope images of the extended and contracted sheaths were of similar appearance, although their lengths were different. The surface lattices of both the extended and the contracted sheaths were determined by optical diffraction. This showed that the quaternary structure of the sheaths of all five defective phages originated from identical surface lattices, which could be approximately expressed by the selection rules L = -2n' + 3m and L = 9N' + 17M for the extended and contracted sheaths respectively, in which 6n' = n with n = 0 or an integer multiple of 6. These results indicated that the packing of the protein subunits in these sheaths differed from those of other bacteriophages, for example T4 and millimicron [Amos and Klug, J. Mol. Biol. 99, 51--73 (1975); Admiraal and Mellema, J. Ultrastruct. Res. 56, 48--64 (1976)]. The molecular weight of the main sheath protein of the defective phages, as determined by dodecylsulphate gel electrophoresis, was approximately 50000. This value differed from that for T4, but was similar to that of millimicron [Admiraal and Mellema, J. Ultrastruct. Res. 56, 48--64 (1976); King and Laemmli, J. Mol. Biol, 75, 315--337 (1973)]. The results of immunodiffusion experiments, however, pointed to a chemical difference between the sheath proteins of the defective phages and millimicron, in addition to T4.
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PMID:The quaternary structure of the sheaths of defective phages similar to PBS X. 10 70

The sup-3 suppressor mutation of Bacillus subtilis has been located between the aroI and mtlB loci by PBS-1 phage transduction.
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PMID:Genetic location of the Bacillus subtilis sup-3 suppressor mutation. 11 Jul 93

Bacteriophage PBS 1 adsorbs initially on the flagella of its host, Bacillus subtilis (stage I). The phage can adsorb to both active and inactive flagella. Flagellar attachment is nonspecific as PBS 1 was shown to attach to the flagella of Bacillus species other than the normal host B. subtilis. The phage particle then quickly moves down the length of the flagellum to its base, the final adsorption site. Flagellar motion is required for flagellar base attachment (stage II). After proper attachment at the flagellar base, the phage tail sheath contracts sending the tail core through the final adsorption site (stage III). The phage DNA is then injected at this site (stage IV). Stage I adsorption does not cause loss of motility in PBS 1 -- resistant bacilli. The loss of motility observed upon infection of sensitive cells by PBS 1 may be associated with either stage II or stage III of adsorption.
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PMID:Adsorption of Bacillus subtilis bacteriophage PBS 1. 11 63

The sensitivity, reproducibility and specificity of an enzyme-linked immunosorbent assay (ELISA) for the defective phage PBS Z1 of Bacillus subtilis have been investigated. It was shown that phages in concentrations between 10(8) and 2.5 X 10(10) particles/ml could be assayed with this method. The coefficient of variation for concentrations between 5 X 10(8) and 5 X 10(9) particles/ml was approx. 10%. From some other Bacillus phages tested, only the defective phages resembling PBS Z1 in morphology were detected efficiently with the ELISA for PBS Z1. A comparison is made between ELISA and other assays for PBS Z1.
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PMID:An enzyme-linked immunosorbent assay (ELISA) for PBS Z1, a defective phage of Bacillus subtilis. 11 36

The structure of the contractile sheath of the defective phage from B. subtilis (PBS-Z) has been investigated by low-dose electron microscopy and image reconstruction. The extended and contracted sheath particles were imaged by means of two negative stains which consisted of uranyl- and phosphotungstate-containing solutions of a pH of 4.2 and 7.0 respectively. Images of identical parts of the same type of specimen were recorded at a total electron dose of 80 C/m2 (5 electrons/A2) and 4 x 10(3) C/m2 (250 electrons/A2). The low-dose reconstructions of the extended and contracted sheath structure in the two stains show good correspondence and made it possible to draw the following structural conclusions. The sheath protein in both types of structure has an elongated shape, and in both structures the long molecular axis lies in a plane perpendicular to the helical sheath axis. The orientation of the protein in the extended and contracted sheath is different; the long axes differ by about 35 degrees in orientation. The reconstructions did not permit conclusions about different conformational states of the protein in both structures. These data, together with the packing parameters of the protein subunits in the contractile sheath [1], form the complete structural analysis of this biological structure by electron microscopy. The radiation damage effects which have been monitored in analyzing image pairs to the full extent may be summarized as follows. (1) Diameters of the sheath structure increase, which indicate flattening. (2) There is no loss in resolution, and layerline altitudes of the Fourier-transformed images do not change. (3) Uranyl stain behaves differently compared to phosphotungstate. In both negative stains the structural noise level increases upon irradiation as follows from the increase in phase residuals of the digital layerline data. In uranyl-stained images also more aperiodic noise appears. (4) The Fourier amplitudes of the principal layerline maxima shift towards lower spatial frequencies; phases of corresponding maxima generally remain constant. This pattern is more pronounced in the extended sheath data; there is no rationale describing these positional shifts. Moreover, in the case of contracted sheath the amplitudes of Fourier components also change more in absolute value. Therefore the damage effects also seem to depend on the type of structure embedded in the stain. (5) In the reconstructed images these radiation effects create artificial stain-excluded volumes of a type and at a radius which depend on the stain and structure.
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PMID:Low-dose electron image reconstruction of negatively stained contractile phage sheath from Bacillus subtilis (PBS-Z). 11 41


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