PubMed Health⌕ Search

Biomedical subjects

N Hiratsuka

Publications and source records attributed to N Hiratsuka.

12 recordsLinked to original sources
PubMed2001

Semiquantitative analysis of urinary low protein levels using silver dot blot assay.

We designed a semiquantitative analysis of urinary low protein levels using silver dot blot assay. In this method, 3 microl of urine are blotted to one dot onto a cellulose acetate membrane, which is stained by a colloidal silver staining reagent, and the optical density of the silver stained urinary protein is measured at 500 nm using a densitometer. There was a good linearity between 2.5 mg/L and 100 mg/L and a gentle linearity between 100 mg/L and 200 mg/L, and the minimum sensitivity was 2.5 mg/L. This method is suitable for semiquantitative analysis of urinary protein levels less than 300 mg/L, which can not be determined precisely by dipstick.

Albuminuria↗
PubMed2001

Degradation of diphenyl ether herbicides by the lignin-degrading basidiomycete Coriolus versicolor.

Under ligninolytic conditions, the white-rot basidiomycete Coriolus versicolor metabolized chloronitrofen (2, 4, 6-trichloro-4'-nitrodiphenyl ether; CNP) and nitrofen (2, 4-dichloro-4'-nitrodiphenyl ether, NIP), which constitute the largest class of commercially produced diphenyl ether herbicides. The pathway of CNP degradation was elucidated by the identification of fungal metabolites upon addition of CNP and its metabolic intermediates. The metabolic pathway was initially branched to form four metabolites--2, 4, 6-trichloro-3-hydroxy-4'-nitrodiphenyl ether, 2, 4-dichloro-6-hydroxy-4'-nitrodiphenyl ether, NIP, and 2, 4, 6-trichloro-4'-aminodiphenyl ether--indicating the involvement of hydroxylation, oxidative dechlorination, reductive dechlorination, and nitro-reduction. Of these reactions, hydroxylation was relatively major compared to the others. Extracellular ligninolytic enzymes such as lignin peroxidase, manganese peroxidase and laccase did not catalyze the oxidation of either CNP or NIP. Piperonyl butoxide, an inhibitor of cytochrome P450, suppressed fungal oxidation of CNP and NIP to their hydroxylated products. The inhibition resulted in increasing the amount of reductively dechlorinated and nitro-reduced products. These observations strongly suggest that basidiomycetes may possess a mechanism for a strict substrate recognition system and a corresponding metabolic response system to effectively degrade environmentally persistent aromatic compounds.

Basidiomycota↗
PubMed1998

Analysis of urinary albumin, transferrin, N-acetyl-beta-D-glucosaminidase and beta2-microglobulin in patients with impaired glucose tolerance.

We investigated the changes in urinary albumin and urinary transferrin as glomerular proteins, and in urinary N-acetyl-beta-D-glucosaminidase and urinary beta2-microglobulin as tubular proteins, in patients with impaired glucose tolerance. We attempted to compare the proteins of normal subjects to those of diabetics with pre-nephropathy. Transferrin and N-acetyl-beta-D-glucosaminidase levels were significantly increased in patients with impaired glucose tolerance, while albumin and beta2-microglobulin levels were only slightly increased. In addition, there was no significant difference in transferrin levels between patients with impaired glucose tolerance and type 2 diabetics with pre-nephropathy. In our observation, although albumin levels were only slightly increased in patients with impaired glucose tolerance, a sharp increase in transferrin levels was reflected in patients with glomerular disorders. In addition, since N-acetyl-beta-D-glucosaminidase levels varied markedly, tubular disorders were suspected. It should be stressed that increased parameters for both glomerular and tubular disorders in group C--patients who showed abnormal levels in three proteins--had already been observed in some patients with impaired glucose tolerance. Therefore, the evaluation of the mutual relationships between various urinary protein components in patients with impaired glucose tolerance will become a more important assessment tool than that of single urinary protein components.

Acetylglucosaminidase↗
PubMed1997

Electrophoretic patterns of urinary proteins of diabetics in the pre, early and overt nephropathy stages.

Urinary proteins of patients with diabetes mellitus (DM) were analyzed using cellulose acetate membrane electrophoresis, to determine the clinical usefulness of fraction patterns of the proteins in detecting the group at high risk for diabetic nephropathy. We divided the protein patterns into 5 groups. Four groups (I, II, III, IV) were found in the healthy group and a newly classified group was termed group 0 and was characterized by a prominent albumin peak with a negligible or small globulin peak. The incidence of groups 0, I, II, III, and IV, was 36.6%, 13.3%, 18.7%, 10.7% and 22.7%, respectively. This distribution was clearly different from that of healthy subjects and the most characteristic feature of diabetics was that group 0 accounted for 36.6% of the total cases. Characteristic features of each group were examined from the aspect of laboratory and clinical findings. Urinary protein patterns were concluded to be useful not only to predict the high risk group for diabetic nephropathy in the preclinical stage but also to discriminate nephropathic types of glomerular or tubular origin. It is useful for clinicians to know the risk stage and prognosis for diabetic nephropathy.

Acetylglucosaminidase↗
PubMed1996

Rapid and highly sensitive colloidal silver staining on cellulose acetate membrane for analysis of urinary proteins.

In order to establish a rapid staining method sensitive enough to stain the protein bands on cellulose acetate membrane and suitable for the analysis of urinary proteins in healthy subjects, we conducted a detailed examination of Kovarik's method designed for the analysis of proteins in cerebrospinal fluid in detail. For purpose, of our study, we changed the pH of the staining solution used in Kovarik's method to pH 4.4 by adding acetic acid. With this solution, our staining method revealed a degree of sensitivity about three times higher than that of the original method, but specific sensitivity for albumin and gamma-globulin remained almost unchanged. The solution preparation we used was much more simple and the reagent much more stable than in the original method. Our method also showed better reproducibility and linearity than the original method. These results point to the suitability of this method for the analysis of low-concentration proteins, such as urinary proteins, in healthy subjects.

Albuminuria↗
PubMed1994

Urinary protein fractions in healthy subjects using cellulose acetate membrane electrophoresis followed by staining with acid violet 17.

We fractionated normal urinary proteins obtained from 40 healthy subjects using cellulose acetate membrane electrophoresis and stained them with Acid Violet 17. The electrophoretic patterns were classified into four groups. Each of groups I, II, III, IV had an albumin peak and 1, 2, 3, and 4 additional globulin peaks, respectively. Within-day variation study showed that the pattern was fundamentally specific to the individual, although some intermediate cases were observed. We were unable to determine which type was standard for normal subjects. However, the concentration of Tamm-Horsfall protein was speculated to be an important factor in determining the patterns. Group III showed significantly higher values than group I in urine albumin, total protein, and beta-N-acetyl-D-glucosaminidase and this group was believed to include subjects in the subclinical stage of a glomerular disease. All specimens belonging to group IV showed an obvious fraction of alpha 1 globulin which is often found in urine specimens of patients with renal diseases of tubular origin or other pathological conditions.

Acetylglucosaminidase↗
PubMed1985

Studies on microcapsules to replace erythrocytes in the passive agglutination reaction.

Two kinds of microcapsules were made from polyurethane and polyurea. Each capsule had a mean diameter of 6 microns, a specific gravity of 1.10, and was red in color. The capsules were coated with ovalbumin condensed with glutaraldehyde. The coated capsules were agglutinated with anti-ovalbumin antibody. The polyurethane capsule (positive charge) bound more ovalbumin and showed a higher sensitivity than did the polyurea capsule (negative charge) or erythrocytes.

Agglutination Tests↗