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Query: UNIPROT:P30536 (PBS)
 9,886 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mouse spleen cells free of erythrocytes were suspended in PBS at a concentration of 2 X 10(7) cells/ml and mixed with an equal volume of sodium periodate in PBS for 10 min. at 4 degrees C to give a final concentration of periodate ranging from 10(-4) M to 5 X 10(-3) M. The cells were then washed and suspended (60 X 10(6) ml) in PBS containing 3H-labelled sodium borohydrate and incubated for 30 min, at 23 degrees C. Following this, the cells were washed and the pellets treated with H2SO4 0.1 N for 60 min. at 80 degrees C. Compounds liberated by such treatment, were identified by chromatography as derivates of sialic acid. The data provide direct evidence that the mitogenic effect of sodium periodate is associated to the oxidation of the sialic acid residues on the lymphocyte membrane.
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PMID:[Periodate oxidation of lymphocyte membrane glycoconjugates]. 20 71

Tissue factor activity was detected in human mononuclear cells cultured with E. coli endotoxin in vitro. The effecient concentration of endotoxin inducing significant tissue factor development was in excess of 10(-3) microgram/ml, and a dose response type relationship was seen between them. The activity developed after culturing for 2 hr and increased up to 6 hr, and thereafter no significant increase was observed. Although the activity was detected both in cell extract and on cell surface, the main activity seemed to exist on the cell surface. No correlation was observed between the synthetic rate of nucleic acid and the rate of development of the activity. Although the activity was detected also in a granulocyte preparation, it was significantly less than that in mononuclear cells. The development of activity was observed when lymphocytes were cultured in RPMI 1640 medium, MEM, and in autologous serum. However, the activity was not observed when cultured in Hanks solution and PBS, in which the main difference from RPMI was the absence of amino acids, and in autologous serum containing sodium citrate which was added for elimination of Ca++ from serum. Moreover, actinomycin D suppressed the development of activity, and the same was noted at low culture temperature. These results suggest that some metabolic change of the cell membrane triggered by endotoxin may induce the development of tissue factor in cells.
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PMID:Development of tissue factor activity in mononuclear cells cultured in vitro. 35 95

"Uncouplers" of oxidative phosphorylation (sodium azide, DNP, and oligomycin) alter the location of microtubules within murine mast cells. Both cytoplasmic microtubules, perpendicular to the plasma membrane within cell surface folds, and intranuclear microtubules were observed. In addition, one or more dense plaque-like structures adjacent the plasma membrane in mast cells appeared following incubation in the antimetabolities. Intranuclear microtubules and cytoplasmic microtubules within the cell surface ridges disappeared in azide-treated mast cells that were reincubated or "recovered" in PBS. However, both these structures remained in oligomycin- and DNP-treated murine mast cells following reincubation.
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PMID:Effect of uncouplers of oxidative phosphorylation on microtubule location and surface structure in murine mast cells. 50 98

This study compares rat spermatozoa with human spermatozoa in respect to disulfide cross links; sulfhydryl group content; and resistance of the structures to chemical agents. The spermatozoa were decondensed, and whole sperm; sperm heads; and tails were counted in a Neubauer chamber and photographed under phase contrast microscopy. The spermatozoa were incubated; centrifuged; and resuspended in PBS for oxidation of sulfhydryl groups. For autoradiography, the spermatozoa were washed in PBS and exposed to a mixture of a maleimide compound and nonradioactive N-ethylmaleimide. Smears were prepared and the slides were developed with Kodak D19 developer. The autoradiograms were then analyzed for distribution and number of grains over the spermatozoa. Upon exposure to dithiothreitol and sodium dodecyl sulfate, human sperm decondensed readily while the rat sperm resisted decondensation for long periods of time. The human sperm exhibited a cooperative effect in the rate of decondensation but not the rat sperm. Oxidation of sulfhydryl groups rendered human sperm as resistant as rat spermatozoa, suggesting the involvement of the disulfide crosslinks in this resistance. Human spermatozoa are a heterogenous population with respect to sulfhydryl group content, indicating variations in the state of maturation and/or elimination. The differences between human and rat spermatozoa as to size; resistance to decondensing agents; cooperative effect during decondensation; and content and localization of sulfhydryl groups explain why vasectomized rats invariably develop huge granulomas while a small percentage of vasectomized men develop small granulomas.
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PMID:Properties of spermatozoa in relation to their elimination after vasectomy. 51 96

The Fc receptor is a plasma membrane component exhibiting an affinity for the C gamma 3 domain of certain subclasses of immunoglobulin G. Using anti-Rho (D)-sensitized red cells (EA) in a slide rosette technique, we have demonstrated a translational mobility and polar redistribution of this receptor on the human blood monocyte and peritoneal macrophage. These cells, isolated from venous blood and malignant ascites and identified histochemically, showed a time- and temperature-dependent receptor capping defined by binding six or more EA confined to the cell half-perimeter. Caps formed in serum were mainly extreme caps in which bound EA appeared as a morula contiguous with the adherent cell. At 21 degrees C and 37 degrees C in serum 80% live rosettes formed caps; virtually none formed at 4 degrees C and about 25% were seen in PBS at 21 degrees C. Similarly, 10% extreme caps in PBS and 60 and 70% in serum were seen at room temperature and 37 degrees C, respectively, suggesting a serum factor(s) was important in promoting live rosette capping. Capping was reversibly inhibited by sodium azide although inhibition was incomplete even at 0.1 M, a concentration 10-fold higher than that giving complete inhibition of lymphocyte antigen-receptor capping. Azide also induced reversion of capped rosettes to diffuse, noncapped rosettes, and to levels comparable to those seen in inhibition studies. Re-exposure to EA after rosette capping failed to increase either the proportion of cells forming rosettes or the fullness of such rosettes indicating a critical number of receptors had been capped. Live rosettes induced a spherocytosis in bound EA irrespective of capping status; such changes appeared early in PBS where capping was minimal. Dead cells bore EA as normal biconcave discs. Some rosetting EA were ultimately hemolyzed upon prolonged incubation, and erythrophagocytosis was seen in about 15% of capped rosettes at 37 degrees C.
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PMID:Redistribution of the Fc receptor on human blood monocytes and peritoneal macrophages induced by immunoglobulin G-sensitized erythrocytes. 127 Aug 3

Sensitive identification of human blood and the determination of ABO blood group from a minute bloodstain were simultaneously carried out by a direct ELISA-ABC method. A cotton thread (1 cm in length) stained with 1 microliter of human or animal blood was stored for 2-4 weeks at room temperature. Hemoglobin (Hb) of the bloodstained thread was gently extracted with 100 microliters of PBS at room temperature, and the thread was washed with PBS to dehemoglobinize. And ABH blood group antigens were extracted from the same dehemoglobinized thread with 100 microliters of 5% ammonia solution at 56 degrees C. The extracts of PBS and ammonia were two-fold serially diluted with 0.1 M sodium carbonate buffer, coated to the wells of a flat bottomed microplate. The PBS extract was tested with a biotinylated antibody against human HbA0 for identification of human blood. Human blood was clearly distinguishable from bloods of other species including Japanese monkey. The minimum detection limit of human blood of the PBS extract of the bloodstained thread was 1:40,960 (3.4 ng Hb), and the limit was found to be approximately 200 times higher than that obtained by a leucomalachite green test or by a precipitation ring test using anti-human HbA serum. The ammonia extract was tested with biotinylated anti-A, anti-B and anti-H antibodies for ABO blood grouping. ABH antigens of the ammonia extract of the bloodstained thread were clearly detected. The minimum determination limits of blood group A, B, AB and O of the ammonia extracts were 1:160, 1:160, 1:80 and 1:160, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Sensitive identification of human blood and simultaneous determination of ABO blood group from a minute bloodstain by an ELISA-ABC method]. 130 54

The stability of pathogenic bacteria from laboratory animals was investigated in various transport media at different temperatures. Bordetella bronchiseptica and Salmonella typhimurium survived for 8 days in phosphate-buffered saline (PBS, pH 7.0) at 37, 24, 4 and -20 degrees C; Brucella canis at 24, 4 and -20 degrees C; Corynebacterium kutscheri at 4 and -20 degrees C; and Pseudomonas aeruginosa at all but -20 degrees C. A marked decrease in numbers of Pasteurella multocida and Past. pneumotropica was observed in PBS at all temperatures. Skimmed milk in PBS improved the survival of Pasteurella spp. and Ps. aeruginosa at -20 degrees C. Neither glycerin, ascorbic acid nor sodium thioglycollate improved survival. The numbers of viable B. canis, Ps. aeruginosa and S. typhimurium were maintained in blood or faecal specimens held for 8 days at 4 degrees C. These results indicated that transport in PBS at 4 degrees C was the only method satisfactory for all species of pathogenic organisms tested, but Pasteurella spp. were the most difficult to maintain.
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PMID:Stability of pathogenic bacteria from laboratory animals in various transport media. 192 20

To reveal the effects of cultural conditions on the cytotoxicity of hexavalent chromium, the uptake of sodium chromate (Na2CrO4) by KB cells and the colony-forming efficiency of the cells were examined under various cultural conditions. The results were summarized as follows: 1) The chromium uptake by the cells after a certain period of incubation with hexavalent chromium was inhibited with the decrease of the temperature (3 degrees, 20 degrees, 37 degrees C), increase of the serum concentration (0, 10, 20, 30%) and increase of pH (6.8-8.2) of the medium. In particular, low temperatures inhibited the chromium uptake by the cells remarkably. However, in relation to the serum addition, no marked effect was found. 2) The chromium uptake by the cells increased with the volume of the medium containing an identical concentration of chromium (2 ppm) and then reached saturation when it was about 0.23 microgram per 10(6) cells. On the other hand, the chromium uptake positively correlated with the concentration of chromium and the total chromium in the medium. 3) The difference of chromium uptake by the cells in different culture media was more marked at acidic pH than that at alkaline pH. However, there was no effect of calcium chloride and glucose concentrations on the uptake of chromium. The chromium uptake by the cells in Ca-Mg-free phosphate-buffered solution (PBS(-] was higher than that in other culture media. Consequently, the above results suggested that the chromium uptake by the KB cells might be affected by the various cultural conditions, especially by temperature, pH and medium volume.
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PMID:[Effects of cultural conditions on hexavalent chromium uptake and the cytotoxicity thereof in KB cell culture]. 209 25

Human alpha 2-macroglobulin (alpha 2M) was eluted as a single nondispersed peak from a TSK-G4000SW size exclusion chromatography column equilibrated in 20 mM-sodium phosphate/100 mM-NaCl, pH 7.2 (PBS). The void volume and total accessible volume of the column were 6.08 ml and 14.42 ml. The elution volume (Ve) of native alpha 2M was 9.20 +/- 0.04 ml. The Ve was altered minimally by changing the ionic strength or adding ethanol to the equilibration buffer. Ternary alpha 2M-trypsin, containing 2 mol of proteinase/mol of inhibitor, and alpha 2M-methylamine failed to be eluted in well-defined peaks when the column was equilibrated in PBS. The majority of either preparation was recovered slowly at Ve values greater than 14.5 ml, reflecting significant nonideal interactions with the support structure. Addition of 10% ethanol or increased ionic strength in the equilibration buffer independently caused either form of reacted alpha 2M to be eluted in a distinct peak at decreased Ve, suggesting that the nonideal interactions included hydrophobic and electrostatic adsorption. When the equilibration buffer was 80 mM-sodium phosphate/320 mM-NaCl, pH 7.2, partial resolution of ternary alpha 2M-trypsin and alpha 2M-methylamine was obtained with a single column run. The Ve values of ternary alpha 2M-trypsin and alpha 2M-methylamine in this buffer were 13.15 +/- 0.08 ml and 11.94 +/- 0.14 ml, respectively. The Ve of native alpha 2M was 8.84 +/- 0.03 ml. The resolving capacity of TSK-G4000SW was exploited to purify native alpha 2M rapidly and efficiently from solutions that contained significant amounts of either ternary alpha 2M-trypsin or binary alpha 2M-trypsin (1 mol of proteinase/mol of inhibitor). This purification was complete within the limits of sensitivity of denaturing and nondenaturing polyacrylamide-gel electrophoresis. alpha 2M-plasmin was well resolved from native alpha 2M. The Ve of alpha 2M-plasmin was 12.88 +/- 0.32 ml in 80 mM-sodium phosphate/320 mM-NaCl, pH 7.2. A number of procedures were used to prepare solutions with up to 90% binary alpha 2M-trypsin. The Ve of binary alpha 2M-trypsin in these various solutions was intermediate between the values of native alpha 2M and ternary alpha 2M-trypsin. The conformations of binary and ternary complex, as reflected by mobility in nondenaturing electrophoresis, were identical, confirming previous results. Finally, in the binary alpha 2M-trypsin complex, the single trypsin cleaved more than two, and as many as all four alpha 2M subunits.
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PMID:Purification and characterization of human alpha 2-macroglobulin conformational variants by non-ideal high performance size-exclusion chromatography. 242 74

Enzyme-linked immunoelectrotransfer blot (EITB) using crude worm antigen of adult Paragonimus westermani was performed for human patients sera to identify the species-specific components. Crude antigen was obtained by homogenizing and centrifuging 24-week old adult worms at 10,000 rpm for 60 minutes in phosphate buffered saline (PBS, pH 7.2) containing phenyl methyl sulfonyl fluoride (PMSF). Gradient sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was performed and blotted electrophoretically onto a sheet of nitrocellulose paper. The sheet was cut into strips and exposed to sera diluted 1: 200 with PBS. SDS-PAGE showed 26 protein bands ranging 229 to 10 kDa. Of them 229, 91, 60, 50, 35-31, 27, 25, 21, 17, 11 and 10 kDa components showed positive reaction with serum antibody of patients with P. westermani. Sera of patients infected with Clonorchis sinensis reacted with 35-31, 19, and 11 kDa bands. Human sera from cysticercosis and diphyllobothriasis cases showed non-specific cross reactions with 229, 35-31, 27, 25 and 17 kDa bands. Protein bands of 91, 60, 21 and 10 kDa showed strong positive reaction without cross reactions with sera from other helminthic infections.
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PMID:Demonstration of species-specific and cross reactive components of Paragonimus westermani crude worm antigen by EITB. 248 66


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