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F Hino

Publications and source records attributed to F Hino.

30 records · Page 2Linked to original sources
PubMed1990

Rapid, simple enzymatic assay of free L-fucose in serum and urine, and its use as a marker for cancer, cirrhosis, and gastric ulcers.

We devised a kit for use with automated analyzers, for assay of urinary free L-fucose by means of a newly isolated L-fucose dehydrogenase (EC 1.1.1.122), and we measured L-fucose in healthy subjects, cancer patients, and patients with other diseases. It takes 10 min to complete one assay. Absorbance and L-fucose concentration were linearly related up to at least 3.0 mmol/L, analytical recovery was 90-104%, and intra- and interassay coefficients of variation were less than 4.2% and 7.8%, respectively. The concentrations of L-fucose, corrected for creatinine, were significantly higher than those in healthy subjects in nine of 18 patients with gastric ulcers, 19 of 21 patients with cirrhosis of the liver, and 206 of 366 patients with some type of cancer, reflecting a changed L-fucose metabolism. Because urine specimens are analyzed and the test is rapid and inexpensive, this method may be suitable for mass screening for some kinds of cancer, cirrhosis, and gastric ulcers.

Adult↗
PubMed1989

Isolation and characterization of two monoclonal antibodies that recognize remote epitopes on the cell-binding domain of human fibronectin.

Two monoclonal anti-fibronectin antibodies that inhibit fibronectin-mediated cell adhesion have been established and characterized. One antibody, FN12-8, inhibited attachment of rat kidney fibroblasts on the fibronectin-coated substrate in a concentration-dependent manner, attaining a maximal inhibition of greater than 85% at 850 micrograms/ml. Another antibody, FN30-8, caused about 70% inhibition at a concentration as low as 0.85 microgram/ml, although further increase of the antibody concentration did not significantly augment the inhibitory effect. Immunoblot analysis with defined proteolytic fragments revealed that both antibodies are directed to the cell-binding domain of fibronectin. The epitopes for these antibodies were further narrowed down using recombinant cell-binding fragments expressed in Escherichia coli. FN12-8 recognized the 11.5-kDa cell-binding fragment previously characterized by Pierschbacher et al. (1981, Cell 26, 259-267), suggesting that FN12-8 blocks the Arg-Gly-Asp (RGD) cell adhesion signal. FN30-8 could not bind this fragment but did recognize a longer cell-binding fragment containing additional greater than 111 amino acid residues upstream of the 11.5-kDa fragment. Since the RGD-dependent cell adhesion seems to require another signal located at a region 50-160 residues upstream of the 11.5-kDa fragment for full activity, FN30-8 may exert its inhibitory effect by blocking the latter signal.

Amino Acids↗
PubMed1982

Effect of 2,4-dichlorophenoxyacetic Acid on glucosylation of scopoletin to scopolin in tobacco tissue culture.

2,4-Dichlorophenoxyacetic acid (2,4-D) stimulated the formation of scopoletin and scopolin in tobacco (Nicotiana tabacum L. ;Bright Yellow') cell culture. It especially stimulated the uptake of scopoletin from culture medium into the cells and the glucosylation of scopoletin to its monoglucoside, scopolin. This phenomenon is peculiar to 2,4-D, in contrast to other plant hormones. 2,4-D (1 mug/ml) stimulated the glucosylation of scopoletin to scopolin by enhancing UDP-glucose:scopoletin glucosyltransferase (SGTase) activity. The enhancement of SGTase activity caused by treatment with 2,4-D was observed when the syntheses of RNA and protein were inhibited by either actinomycin-D and/or cycloheximide. However, the stimulatory effect of 2,4-D was inhibited by treatment with dinitrophenol. Furthermore, SGTase with or without treatment by 2,4-D in vivo for 24 hours, was isolated from cultured tobacco cells. The enzymes were purified about 200-fold by precipitation with (NH(4))(2)SO(4) and chromatography with Sephadex G-100, DEAE-cellulose, and hydroxyapatite. The specific activity of 2,4-D-treated SGTase was 10 times higher than that of untreated SGTase even in the purified fraction, which showed one protein band under electrophoresis. These results suggest that the enhancement of SGTase activity by 2,4-D is due to the energy-dependent activation of the enzyme already present, but not due to the de novo synthesis of the enzyme.

Journal Article↗