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Biomedical subjects

H Nomoto

Publications and source records attributed to H Nomoto.

At least 73 records · Page 4Linked to original sources
PubMed1985

A sensitive two-site enzyme immunoassay for human epidermal growth factor (urogastrone).

A sensitive enzyme immunoassay (EIA) was developed for human epidermal growth factor (hEGF) or urogastrone, which was isolated from human urine. Our EIA system is based on the sandwiching of an antigen between anti-hEGF IgG coated on a polystyrene tube and anti-hEGF antibody Fab'-linked beta-D-galactosidase (beta-D-galactosidase, EC 3.2.1.23). This method has the advantages that the procedures are simple and rapid and that the antibody Fab'-beta-D-galactosidase complex is more stable than radioisotope-labeled IgG. Purified hEGF is detectable at as low as 100 pg/ml, which is very sensitive compared to the radioimmuno-assays or radioreceptor assays already reported. Using this new EIA system, hEGF levels in human urine were examined. The values for normal males and females were 48.4 and 83.5 ng/mg creatinine, respectively, which shows that females excrete 1.7 times more hEGF than males.

Electrophoresis, Polyacrylamide Gel↗
PubMed1985

Cold-reacting antinuclear factor in sera from patients with primary glomerular diseases.

Antinuclear factor (ANF) was determined in sera from patients with primary glomerular diseases to evaluate the autoimmune nature of this disorder. Sera from 61 patients with various types of glomerular disorders were assayed for ANF by the fluorescent antinuclear antibody (FANA) technique at 37 degrees C and 4 degrees C. Thirty healthy adults served as controls. Cold-reacting ANF, which was detected predominantly in the class of IgM, was observed in 54 out of 61 patients with various types of primary glomerular disorders. The nuclear staining pattern was "speckled". Sera from healthy adults did not show any positive signs of ANF. It is suggested that some autoimmune mechanisms may be involved in the development of primary glomerular diseases.

Adolescent↗
PubMed1984

Novel oligosaccharide chains on polysialoglycoproteins isolated from rainbow trout eggs. A unique carbohydrate sequence with a sialidase-resistant sialyl group, DGa1NAc beta 1 leads to 4(NeuGc2 leads to 3)DGa1NAc.

A series of novel carbohydrate chains all possessing a hitherto unknown trisaccharide unit, Ga1NAc beta 1 leads to 4-(NeuGc2 leads to 3)Ga1NAc beta 1 leads to, have been isolated from trout egg polysialoglycoproteins, a new class of glycoproteins, on alkali-borohydride treatment. On the basis of chemical (methylation, Smith degradation, and hydrazinolysis-nitrous deamination) and direct-probe mass spectrometric methods. deamination) and direct-probe mass spectrometric methods, the structures of a series of the first major type of oligosaccharide alditols having a sialidase-resistant N-glycolyneuraminic acid residue in each molecule were determined. The structures thus determined are novel and all possess a unique carbohydrate sequence (sialidase-resistant unsubstituted sialyl group italicized): Ga1NAc beta 1 leads to 4(NeuGc2 leads to 3)Ga1NAc beta 1 leads to 3Gal beta 1 leads to-4Gal beta 1 leads to 3[(leads to 8NeuGc alpha 2)n leads to 6]Ga1NAcol (n = 0 through 3).

Animals↗
PubMed1984

Fish egg polysialoglycoproteins: circular dichroism and proton nuclear magnetic resonance studies of novel oligosaccharide units containing one sialidase-resistant N-glycolylneuraminic acid residue in each molecule.

Long-core units having the common sequence Ga1NAc beta 1 leads to 4(NeuGc2 leads to 3)Ga1NAc beta 1 leads to 3Gal beta 1 leads to 4Ga1 beta 1 leads to 3Ga1NAc are one of the major constituents of rainbow trout egg polysialoglycoproteins. The existing ambiguity regarding the anomeric configuration of the sialidase-resistant unsubstituted sialyl group present in this novel type of oligosaccharide chains has been resolved by a circular dichroism difference spectral method. The fact that the negative band originating from the carbohydrate n leads to pi transition for this sialyl group was observed offers conclusive proof of the alpha-anomeric configuration. Next particularly interesting is the fact that the chemical shifts of the sialidase-resistant sialyl H-3eq and H-3ax protons were respectively found at relatively higher and lower magnetic field than for the corresponding protons of other sialyl groups. A consideration of molecular models shows that the observed anomalies are all in the directions compatible with expectations on the basis of the magnetic anisotropy effect due to the carboxylate group and steric compression effects by van der Walls interactions between groups that are sterically compressed. In addition to the observed resistance to bacterial sialidases of this sialyl group, it did not behave even as a competitive inhibitor of the sialidase, Arthrobacter ureafaciens, indicating that inaccessibility of this unique sialyl group toward the enzyme. Finally, the analysis of the proton nuclear magnetic resonances of sialidase-sensitive mono- and oligosialyl groups present in the long-core units was based on comparisons of diagnostically important regions in the spectra of homologous oligosaccharides of N-glycolylneuraminic acid.

Animals↗
PubMed1984

Selective urinary excretion of phosphatidyl ethanolamine in patients with chronic glomerular diseases.

Urinary phospholipids and lipoproteins in chronic glomerular diseases were analyzed. The subjects used were 26 patients consisting of 14 with chronic glomerulonephritis and 12 with nephrotic syndrome. Nine healthy normals served as controls. Phospholipids were isolated by one-dimensional thin-layer chromatography (TLC) using an internal standard for quantification and partially by two-dimensional TLC and, furthermore, quantified by two different methods to ascertain the kinds of phospholipids. Urinary lipoproteins were isolated by density gradient ultracentrifugation and analyzed by electrophoresis. The urinary excretion of phosphatidyl ethanolamine (PE) was recognized exclusively in the patient group and that of phosphatidyl serine (PS) in most cases with nephrotic syndrome. The daily urinary PE excretion rate was closely correlated to the urinary albumin excretion rate. However, phosphatidyl choline (PC) and sphingomyelin (SPH), which are main phospholipids in serum and red blood cell membranes, in most cases were hardly detected in urine. These observations were confirmed by two-dimensional TLC using valuable spot tests for identification of phospholipids and also by the two different quantification methods. In density gradient ultracentrifugation, urinary lipoproteins did not form such peaks as seen in the profiles of serum lipoproteins. The presence of urinary lipoproteins in two nephrotic patients has been shown, but although the method used was not very sensitive, it was suggested that lipoproteins were hardly excreted into urine as the lipoprotein deficient fraction (LPDF) (d greater than 1.21 g/ml), in which albumin is predominant. PE was found mainly in LPDF of urine, although the amount of PE in urinary lipoproteins was very limited.(ABSTRACT TRUNCATED AT 250 WORDS)

Adolescent↗
PubMed1984

Isolation and structures of the third major type of carbohydrate units in polysialoglycoproteins from rainbow trout eggs.

The structures of the third major type of oligosialyloligosaccharides obtained by alkali-borohydride treatment of polysialoglycoproteins of the unfertilized eggs of rainbow trout have been determined to be: alpha-L-fucosyl-(1----3)-beta-N-acetyl-D-galactosaminyl-(1----3)-beta-D- galactosyl-(1----4)-beta-D-galactosyl-(1----3)-[[(----8)-alpha-N- glycolylneuraminyl-(2----)]n-(----6)]-N-acetyl-D-galactosaminitol with n = 1 to 4. The proportion of the fucose-containing units in 3 major carbohydrate units present in fish egg polysialoglycoproteins was found to be highly species-specific and only 6% in the eggs of rainbow trout.

Animals↗
PubMed1983

A novel glycoasparagine isolated from an ovalbumin glycopeptide fraction (GP-IV). Anion-exchange borate chromatography and structural analysis of GP-IV glycoasparagines.

The fraction GP-IV obtained from hen ovalbumin has been further fractionated on DEAE-Sephadex A-25 in borate buffer, a new system for the separation and isolation of glycoasparagines on columns. The structures of one major and two minor glycoasparagines thus obtained were determined by enzymatic (endo-beta-N-acetylglucosaminidase D and H digestion), chemical (modified Smith degradation, acetolysis, and methylation analysis), and instrumental (270 MHz 1H nuclear magnetic resonance spectroscopy) analyses. The following structure is novel for carbohydrate moieties in ovalbumin glycoasparagines: (formula; see text) The present anion exchange chromatography in borate solution is well suited for separating and preparing oligosaccharides having similar molecular size but differing in content of vicinal cis-diol group.

Animals↗
PubMed1983

[Clinical investigation of combined therapy (cefotiam, sulbenicillin and cefsulodin) against infections complicated by acute leukemia].

Prophylaxis effect and clinical therapy of combination use of cefotiam (CTM), sulbenicillin (SBPC) and cefsulodin (CFS) have been investigated, and the results were as follows. 1. Prophylaxis effect of CTM-SBPC combination therapy was very useful. CTM-SBPC combination therapy was performed to patients who are at high risk for infectious complications. Prophylaxis effect of CTM-SBPC was judged by fever over 38 degrees C, and was better than usual antibiotic treatment. 2. CTM-SPBC-CFS combination therapy was performed against severe infections during early remission, and the overall effectiveness rate was 83.3% (5/6). 3. No remarkable side effect was observed in this investigation.

Acute Disease↗
PubMed1982

Preparation and characterisation of fragment glycoasparagines from ovalbumin glycopeptides: reference compounds for structural and biochemical studies of the oligo-mannose and hybrid types of carbohydrate chains of glycoproteins.

Glycoasparagines obtained after exhaustive digestion by Pronase of purified ovalbumin were partially degraded by trifluoroacetic acid or subjected to Smith degradation. The partially degraded glycoasparagines thus obtained were first fractionated according to molecular size on Dowex 50W-X2 and then further fractionated by borate chromatography on a column of Sephadex A-25. For a mixture of glycoasparagines of similar molecular size, the latter procedure fractionates according to increasing content of mannosyl cis-2,3-diol. Ten fragment glycoasparagines have been prepared from ovalbumin glycoasparagines, and the structures determined by 1H-n.m.r. spectroscopy and methylation analysis.

Animals↗