Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0009443 (cold)
 92,137 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hydrosoluble substances from BCG were prepared by cold water extraction and by hot phenol-water extraction. Chemical analyses revealed that both of them were derived from cytoplasm. The cold water extract (CWE) was effective in the treatment of C3H/He mice which had received an intraperitoneal inoculation of a syngeneic ascites hepatoma, MH134. The growth of a graft in footpad of mastocytoma P815 in CDF1 mice was retarded by intraperitoneal injections of CWE. A peptidoglycan from cell wall prepared by digestion with lysozyme exerted no antitumor activity in the same experimental condition as for the evaluation of antitumor effect of CWE. These results indicate that the antitumor activity of CWE was not due to the presence of a cell wall component.
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PMID:Chemical analyses and antitumor activity of hydrosoluble substances from Mycobacterium bovis, strain BCG. 619 9

Before attempting to radiolabel proteins it is essential that conditions be found for optimal reaction by use of cold reagents. Iodination by the chloramine-T method was not suitable for radiolabeling of lysozyme as it resulted in reduced solubility, large conformational changes, loss of enzymic activity and a decrease in immunochemical reactivity. On the other hand, reductive methylation of lysozyme by formaldehyde and sodium cyanoborohydride was considered suitable for radiolabeling of lysozyme. The extent of reaction with the free amino groups was dependent on the concentration of lysozyme and the molar ratios of the reactants (lysozyme, NaCNBH3 and HCHO). The molecular weight, net charge and enzymic activity of the lysozyme derivatives were similar to the native molecule. The immunochemical reactivity was reduced by 6-13% when more than 6 amino groups were modified. Reductively methylated rabbit IgG showed unaltered molecular weight, net charge and very little conformational changes compared to native IgG. Partial reaction, by reductive methylation using [14C]HCHO, lysozyme with specific activity of 11.1 X 10(6) cpm/mg protein and pig anti lysozyme antibody with specific activity of 2.95 X 10(5) cpm/mg protein were prepared.
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PMID:Comparative studies on radiolabeling of lysozyme by iodination and reductive methylation. 665 44

Polymyxin-resistant pmrA mutants of Salmonella typhimurium differed from their parents in that they were resistant to tris(hydroxymethyl)aminomethane-ethylenediaminetetraacetate-lysozyme, tris(hydroxymethyl)aminomethane-ethylenediaminetetraacetate-deoxycholate, and tris(hydroxymethyl)aminomethane-ethylenediaminetetraacetate-bacitracin. Tris(hydroxymethyl)aminomethane-ethylenediaminetetraacetate released about 50% less lipopolysaccharide from the pmrA strains than from the parental strains when the bacteria were grown in L-broth containing 2 mM Ca2+. Protamine, polylysine, octapeptin, benzalkonium chloride, cold NaCl, cold MgCl2, or cold tris(hydroxymethyl)aminomethane hydrochloride (pH 7.2) caused no leakage or markedly less leakage of periplasmic beta-lactamase from a pmrA mutant than from its parent strain. pmrA mutants were more resistant than their parent strains to protamine and polylysine but not to octapeptin or benzalkonium chloride, as measured by the ability of these agents to kill the bacteria or to sensitize them to deoxycholate-induced lysis. The pmrA strains did not differ from their parent strains in sensitivity to several antibiotics, in porin function (as measured by cephaloridine diffusion across the outer membrane), or in outer membrane-associated phospholipase A activity.
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PMID:Increased outer membrane resistance to ethylenediaminetetraacetate and cations in novel lipid A mutants. 679 77

Light and electron microscopy of neutrophils from chronic neutrophilic leukemia (CNL) did not reveal differences from normal mature neutrophils. However, functional characterization of CNL cells showed marked differences when compared to normal cells. CNL neutrophils were much less viable in suboptimal conditions. Their survival was further reduced by autologous serum and was corrected by normal human serm. CNL cells showed very active phagocytosis, but their bactericidal activity was reduced in suboptimal conditions. The total content of lysozyme and beta-glucuronidase was lower in CNL cells compared to normal neutrophils, but the release of these enzymes from stimulated cells was much higher than normal. This observation is compatible with a marked lysosomal lability. Cells from the patients' peripheral blood and bone marrow showed excessive growth in CFU-C assays. Marked susceptibility of CNL cells to cytotoxic activity of cold agglutinins, SLE sera, and CSFs was observed and may signify qualitative and/or quantitative differences in the membrane structure of CNL neutrophils, as compared to normal cells.
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PMID:Functional characterization of the cells in chronic neutrophilic leukemia. 704 35

Salt treatment of the cytoplasmic estradiol-receptor complex from chick oviduct induces a strong affinity of the complex for DNA-cellulose and phenyl-sepharose. This process is called activation. Binding to heparin- and lysozyme-sepharose is also observed with the untreated complex. But, the salt treatment, additional binding of the complex to these adsorbents is seen. The increased ability of the complex to bind to polyanions and polycations is destroyed by mild trypsination. The binding to the hydrophobic adsorbent is not affected by this treatment. Neither a change of the sedimentation constant nor of the size of the receptor protein is observed after salt treatment in the cold. After binding of the salt-activated estradiol-receptor complex to DNA-cellulose in the cold, an increase of its sedimentation constant and its size, as measured by density-gradient centrifugation and agarose gel chromatography, resp., becomes apparent. A similar phenomenon is observed after binding to DEAE-cellulose and to some extent after binding to heparin-sepharose. The nuclear complex seems to have the same sedimentation constant as the cytoplasmic complex eluted from DNA-cellulose. The sedimentation constant of the nuclear complex is not changed after DNA-cellulose chromatography. The cytoplasmic progesterone-receptor complex from the same tissue, i.e. the oviduct, does not show any change of size. Thus the well-known process of transformation can now be separated into 2 steps. (1) Activation of the estradiol-receptor complex for its binding to various adsorbents in vitro and probably to its acceptor site(s) in vivo. (2) Increase of receptor size. This second step seems to be a special property of the estradiol-receptor complex. Its physiological significance is unclear.
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PMID:Transformation of the estrogen-receptor complex from chick oviduct in 2 steps. 720 34

Streptococcus mutans BHT was grown in Todd-Hewitt dialysate medium containing N-acetyl[(14)C]glucosamine for 6 to 11 generations. After treatment with cold and hot trichloroacetic acid and trypsin, 52 to 65% of the radioactivity remained present in insoluble peptidoglycan-containing residues. Hen egg white lysozyme or mutanolysin treatment of the peptidoglycan residues resulted in the release of 80 and 97%, respectively, of the (14)C label to the supernatant fraction. Hydrochloric acid hydrolysates of such supernatants showed that essentially all of the radioactivity present in insoluble peptidoglycan fractions was present in compounds that comigrated on paper chromatography with glucosamine ( approximately 60%) or muramic acid ( approximately 30%). Treatment of whole cells with low and high concentrations of lysozyme alone resulted in losses of 45 and 70% of the insoluble peptidoglycan, respectively, yet release of deoxyribonucleic acid from cells was not detected. Sequential addition of appropriate concentrations of selected inorganic salts after lysozyme treatment did result in the liberation of deoxyribonucleic acid. Deoxyribonucleic acid release was correlated with a further release of peptidoglycan from the insoluble fraction. However, the total amount of peptidoglycan lost effected by the low concentration of lysozyme and NaSCN (lysis) was significantly less than the amount of peptidoglycan hydrolyzed by high concentrations of lysozyme alone (no lysis), suggesting that the overall amount of peptidoglycan lost did not correlate well with cellular lysis. The total amount of insoluble peptidoglycan lost at the highest salt concentrations tested was found to be greater than could be accounted for by lysozyme-sensitive linkages of the peptidoglycan, possibly implicating autolysins. The results obtained suggested that hydrolysis of peptidoglycan bonds in topologically localized, but strategically important, sites was a more significant factor in the sequence that results in loss of cellular integrity (lysis).
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PMID:Peptidoglycan loss during hen egg white lysozyme-inorganic salt lysis of Streptococcus mutans. 721 16

Activation of the alternative pathway of complement is known to be initiated by bacterial structures. We have fractionated Propionibacterium acnes cells, purified various cell fractions, and tested their complement-activating ability in human serum chelated with ethyleneglycol bis-(beta-aminoethylether)-N,N1-tetraacetic acid. The majority of complement-activating activity was localized in the wall fraction. This activity was resistant to lipid extraction, protease, RNAse, DNAse and lysozyme treatment. NaIO4, formamide, and hot (but not cold) trichloroacetic acid (TCA) extraction ablated the complement-activating capacity of cell walls. Compounds removed by extraction failed to consume significant hemolytic activity against antibody-coated sheep erythrocytes (EA). Addition of TCA-extracted soluble material to cell wall suspensions resulted in an inhibition of hemolytic consumption by the cell wall. These results indicate that, in P. acnes, complement-activating molecules are located in the cell wall and are carbohydrate in nature. Peptidoglycan, lipid, protein, and nucleic acid do not appear to contribute to the cell wall's ability to activate complement.
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PMID:Activation of the alternative pathway of complement in human serum by Propionibacterium acnes (Corynebacterium parvum) cell fractions. 727 77

The present study was undertaken to elucidate the relationship between the distribution of potentially proliferative tumor cells and the organoid differentiation of tumor cells in gastric carcinomas. One hundred four specimens of surgically removed human gastric carcinomas, including 68 and 36 specimens of early and advanced carcinomas, respectively, were studied by using a battery of histochemical techniques. Serial 3-microns thick paraffin sections were stained by galactose oxidase-cold thionine Schiff-paradoxical concanavalin A staining (GOCTS-PCS), or were immunostained for pepsinogen types I and II, lysozyme, and proliferating cell nuclear antigen (PCNA). In addition, to identify proliferative tumor cells parts of fresh carcinoma tissues were incubated in a solution containing bromodeoxyuridine (BrdU), embedded in paraffin, and immunostained for BrdU. The results indicated that in intramucosal carcinoma tissues showing organoid differentiation the proliferative tumor cells were located predominantly between the covering epithelial cell type tumor cells and the glandular mucous cell type tumor cells, and the disturbance in the distribution of proliferative cells coincided with the submucosal invasion.
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PMID:Proliferative markers in gastric carcinoma and organoid differentiation. 762 43

A high level production system for heterologous protein by cold culture of yeast transformants at 15 degrees C was developed. The yeast transformants, carrying a plasmid containing cDNA for Aspergillus oryzae alpha-amylase (Taka-amylase A) or human lysozyme synthetic DNA, were cultivated in a selective medium for 1 or 2 days until full growth at 30 degrees C. The yeast cells were harvested by centrifugation from the culture fluid and then were transferred to YPD medium. These inoculated broths were incubated for 2 days at 15 degrees C and then for another 2 days at 30 degrees C. By the cold culture method described above, higher amounts of Taka-amylase A (28.6 mg/liter) and human lysozyme (6.1 mg/liter) were produced by the yeast transformants compared to those by conventional methods. Heterologous protein productions using YEp, YCp, and YIp types of yeast expression vectors with ADH1 or GAPDH promoter by the cold culture method showed effective productivity of about 2-fold compared to those by the conventional method of culture at 30 degrees C. The high level production of heterologous protein by this method was not specific to the S. cerevisiae strains examined.
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PMID:A novel culture method for high level production of heterologous protein in Saccharomyces cerevisiae. 776 52

Cell wall turnover appeared to be anomalously fast in Bacillus subtilis when the cells were grown at temperatures below 29 degrees C. Turnover rates k(generation-1), of exponential cultures at 25 degrees were approximately double those of cells grown at 37 degrees C. When autolysin levels were assayed in cell walls, it was found that the enzyme activities were constant between 25 degrees C and 40 degrees C, suggesting that there was no greater synthesis of autolysin at the lower temperature. Analyses of walls for individual components, extent of aminosugar substitution and extent of crosslinking, did not reveal significant differences between samples obtained from 25 degrees C or 37 degrees C cultures. The N-acetylmuramoyl-L-alanine amidase was stable over the temperature range studied. Lysis of cells, induced by carbonylcyanide-m-chlorophenylhydrazone, occurred at a faster rate for cells obtained at 25 degrees C than for cells obtained at 37 degrees C. In addition, the lysis of cells by hen egg white lysozyme was slightly faster when the cells were obtained from 25 degrees C cultures than from 37 degrees C cultures. It is possible the autolysin(s) responsible for cell wall turnover are cold-activated.
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PMID:Anomalies in cell wall turnover associated with the growth temperature of Bacillus subtilis. 809 13


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