Search PubMed⌕ Search

Biomedical subjects

H Fukushima

Publications and source records attributed to H Fukushima.

At least 289 records · Page 16Linked to original sources
PubMed1987

Determination of ABO blood groups by radioimmunoassay using 125I-protein A.

Since the crystallizable fragment (Fc) portion of the immunoglobulin G (IgG) molecule is the binding site of Protein A, a radioimmunoassay procedure using 125I-Protein A was developed for identification of the ABO blood groups. The isotope level bound to Group A, B, or AB red cells decreased with the dilution of anti-A or -B, respectively. After sensitization by anti-A plus B in Group O serum, the isotope bindings were observed in Groups A, B, and AB cells, while no significant radioactive count appeared in Group O cells. Furthermore, there was little significant isotope binding in both Group A and B red cells sensitized by the serum from Group A or B blood containing mainly IgM anti-A or -B. A radioimmunoassay using 125I-Protein A is an excellent method for identifying ABO blood groups.

Blood Group Antigens↗
PubMed1987

Mouse anti-benzylpenicilloyl IgE monoclonal antibody: preparation, characterization and cross-reactivity.

Anti-benzylpenicilloyl (BPO-) monoclonal antibody of the IgE class was prepared from spleens of immune C57BL/6 mice whose sera reacted with BPO-hapten, penicillin G(PCG) polymer, cephalothin (CET)-hapten and CET polymer. Affinity chromatography experiments showed that the haptenic specificity of the IgE monoclonal antibody (designated BIE-13CE) was directed mainly to phenylacetyl portion of BPO group. BIE-13CE antibody reacted on passive cutaneous anaphylaxis (PCA) assay with BPO-hapten, CET-hapten, cephaloridine-hapten and CET polymer, but did not react with PCG polymer, ampicillin-hapten, or cefazolin-hapten. These results indicated that the sera of the immune C57BL/6 mice contained IgE antibodies capable of cross-reacting at the monoclonal antibody level with various forms of eliciting antigens and that the cross-reactivity of the antibody could be ascribed essentially to the structural similarity of acyl side chains of the antibiotics. The structure of the CET polymer is also discussed in terms of its PCA reactivity with the monoclonal antibody and analytical and spectral data of the polymer.

Animals↗
PubMed1986

Quantitative comparison of Rh1 (Rho, D) antigen on D, Du and d red cells by radioimmunoassay using 125I-protein A.

Relative Rh1 (Rho, D) antigen contents of the red Rh: 1 (Rh positive, D), Rh: wl (Rh variant, Du) and Rh: -1 (Rh negative, d) cells were estimated from the quantity of 125I-protein A bound to the sensitized red cells. The isotope binding activity to both D and Du cells decreased in parallel with the dilution of anti-D serum. The relative amount of the 125I-protein A bound to Du cells was about one-sixth that of D cells without papain treatment, while no isotope binding was observed in d cells. The Du red cells were quantitatively deficient in Rh1 (Rho, D) antigen activity compared with the D cells. A radioimmunoassay using 125I-protein A was a very useful method for studies regarding measuring the relative amounts of various blood group antigens.

Erythrocyte Membrane↗
PubMed1986

Suppression of heat-stable enterotoxin production by Yersinia spp. in milk.

One of 16 raw milk isolates of Yersinia enterocolitica and Y. intermedia produced heat-stable enterotoxin (ST) in milk at 25 degrees C but not at 4 degrees C after 21 days of incubation. A catabolite repression of ST synthesis by the lactose-fermenting strain of Y. enterocolitica was observed when 4.6% lactose was added to trypticase soy broth. However, the lactose-fermenting strain was killed by acid produced by lactose fermentation in milk and did not produce ST in milk with the pH adjusted to neutrality. This study suggested that lactose and fat in milk are not the fundamental inhibitors of ST synthesis by Y. enterocolitica and that repression of ST synthesis may be related to other components.

Animals↗
PubMed1986

Inhibition of Yersinia enterocolitica serotype O3 by natural microflora of pork.

Yersinia enterocolitica serotype O3 did not grow but did survive in inoculated raw ground pork kept at 6 and 25 degrees C. The antagonistic effect of microbial flora, especially Hafnia alvei and environmental Yersinia organisms, on the growth of Y. enterocolitica serotype O3 in raw ground pork was evident. These results were supported by evidence of the inhibition of growth of Y. enterocolitica serotype O3 by Enterobacteriaceae, especially H. alvei and environmental Yersinia organisms, in mixed cultures at 6 and 25 degrees C. We suggest that naturally contaminated pork is a source of human infection, since Y. enterocolitica serotype O3 was capable of surviving in the raw pork for a long time.

Animals↗
PubMed1986

Growth of Yersinia pseudotuberculosis and Yersinia enterocolitica biotype 3B serotype O3 inhibited on cefsulodin-Irgasan-novobiocin agar.

A total of 169 strains of Yersinia spp. were analyzed for their ability to grow on two different kinds of cefsulodin-Irgasan-novobiocin (CIN) agar containing 15 or 4 micrograms of cefsulodin per ml, on salmonella-shigella agar, and on MacConkey agar. CIN media inhibited the growth of Yersinia pseudotuberculosis and Yersinia enterocolitica biotype 3B serotype O3 (3B/O3) but not the growth of the other Yersinia organisms used. Relative to growth on Trypticase soy agar (BBL Microbiology Systems, Cockeysville, Md.) with 6% yeast extract, 48 and 44% of Y. pseudotuberculosis and Y. enterocolitica 3B/O3 strains, respectively, were inhibited on CIN I agar (low cefsulodin concentration), and 83 and 54%, respectively, were inhibited on CIN II agar (high cefsulodin concentration) after incubation for 24 h at 32 degrees C. The inhibition of Y. pseudotuberculosis growth was significantly more extensive on CIN II agar than on CIN I agar. The MICs of cefsulodin and novobiocin clearly indicated a higher susceptibility for Y. pseudotuberculosis than for the other Yersinia organisms at 32 degrees C. All Y. pseudotuberculosis strains were susceptible to cefsulodin at 15 micrograms/ml (the approximate concentration used in CIN II agar). Y. enterocolitica 3B/O3 strains were resistant to cefsulodin, Irgasan, and novobiocin at the concentrations used in CIN media. These findings show that cefsulodin inhibits the growth of Y. pseudotuberculosis at the concentration used in CIN media and that growth inhibition of Y. enterocolitica 3B/O3 is related to a component of the CIN Base.

Agar↗
PubMed1986

Chromosome 1 localization of the human alpha-L-fucosidase structural gene with a homologous site on chromosome 2.

Two cDNA clones coding for human alpha-L-fucosidase, one from the coding region and the other primarily from the 3' untranslated region, were used to map the location of the alpha-L-fucosidase gene. Southern filter analysis of somatic cell hybrid lines mapped the structural gene to the short arm of human chromosome 1, and in situ hybridization to chromosomes of human leukocytes further localized the homologous area to the 1p36.1----p34.1 region, with the most likely location being the distal region of 1p34. Further Southern filter analysis detected a second site of homology on chromosome 2. This alpha-L-fucosidase-like site has been designated FUCA1L.

Animals↗
PubMed1985

Characterization and mode of action of a purified bacteriocin from the oral bacterium Streptococcus mutans RM-10.

The purified bacteriocin was sensitive to proteolytic enzymes such as trypsin, alpha-chymotrypsin and pronase, but resistant to papain and pepsin. Lowering the pH of the bacteriocin caused precipitation, and the Abs280 of the supernatant reached a minimum at pH 3.6, suggesting that this is the isoelectric point. Such a pH value coincides with minimum bacteriocin activity. The effect of the bacteriocin was bactericidal rather than bacteriolytic and concentration dependent. Treatment of Streptococcus faecalis ODU with Rm-10 bacteriocin led rapidly to the cessation of biosynthesis of macromolecules, DNA, RNA and protein. Electron microscopy showed bacteriocin fibres attached in aggregated bundles to target cells; after ultra-sonication or detergent treatment they were individually attached to the cell surface and, at the same time, the apparent bacteriocin activity had doubled. Bacteriocin activity was not altered by filter-sterilized saliva components. Oral rinsing with Rm-10 bacteriocin reduced the number of viable salivary bacteria after 20 min, suggesting a possible therapeutic use for Rm-10 bacteriocin.

Animals↗
PubMed1985

Comparison of the immunochemical responses by anti-NADPH-cytochrome c reductase of Tetrahymena pyriformis (strain NT-1) in protozoan cells and mammalian liver microsomes.

Comparison of the microsomal NADPH-cytochrome c reductase activities in the four Tetrahymena cells (pyriformis, strain GL and NT-1; thermophilia; ISO) and rat liver was studied. The reductase activity in strain NT-1 was lowest among four Tetrahymena cells grown at 24 degrees C. Rabbit antibody was prepared against the purified NADPH-cytochrome c reductase from Tetrahymena pyriformis (strain NT-1) microsomes. Microsomal NADPH-cytochrome c reductase activities in various Tetrahymena cells were inhibited in proportion to the amount of antibody added, in the order of GL greater than NT-1 greater than thermophilia greater than ISO. No inhibition of reductase activity by antibody was observed in rat liver microsomes.

Animals↗
PubMed1985

Membrane proteins in Rh+, Rh- and Rh: -29, 38 (- - -/- - -, rh) red cells compared by using SDS-polyacrylamide gel electrophoresis.

Since Rh: -29, 38 (- - -/- - -, rh) phenotype of the Rh blood groups (--- in text) revealed unusual red cells, such as stomatocytes and microspherocytes and the relatively shortened half life of 17 days, red cell membrane proteins from Rh + (D), Rh - (d) and --- were compared by using SDS-polyacrylamide gel electrophoresis (SDS-PAGE). No differences were observed among the patterns of the reduced and non-reduced membrane proteins from Rh+, Rh- and --- red cells. Two-dimensional gel electrophoresis of --- red cell membrane proteins also revealed a pattern similar to Rh+ and Rh- red cell membrane proteins. It is suggested that the lack of all Rh antigens causes no visible alteration of red cell membrane proteins detected by the method of Fairbanks G., Steck T.L. and Wallach D.F.H. (1971) Biochemistry, N.Y. 10, 2606-2617.

Electrophoresis, Polyacrylamide Gel↗