PubMed Health⌕ Search

Biomedical subjects

N Kohashi

Publications and source records attributed to N Kohashi.

5 recordsLinked to original sources
PubMed1992

[Quality of the life in hypertensive outpatients].

In order to evaluate the quality of life (QOL) in hypertensive outpatients, we selected 78 patients with hypertension of various degrees of severity (WHO Classification I: 29 cases, II: 15, III: 34), 59 not ill healthy persons (N1) and 22 normotensive outpatients (N2) aged at 50 years and over, using the self-completed questionnaire (QUIK) which we developed. QUIK covers four domains including physical functioning (20 questions), emotional adjustment (10), interpersonal relationships (10) and attitudes toward life (10) totaling 50 questions. In this study the internal consistency of QUIK was alpha = 0.95 by the Kuder-Richardson formula 20 and it's repeatability was r = 0.89 by the Spearman-Brown formula. The QOL in hypertensive outpatients was definitely worse in terms of total score (N1 5.1 +/- 4.4 vs WHO II 9.3 +/- 7.2 and III 12.1 +/- 5.6, p < 0.05), for physical functioning (N1 2.5 +/- 2.1 vs WHO I 3.7 +/- 2.8, II 4.7 +/- 3.8, III 5.4 +/- 2.8 p < 0.05), for emotional adjustment (N1 1.2 +/- 1.4 vs WHO III 2.3 +/- 1.7, p < 0.01), for interpersonal relationships (N1 0.8 +/- 1.3 vs WHO III 1.6 +/- 1.5, p < 0.01) and for attitudes toward life (N1 0.7 +/- 1.2 vs WHO III 2.7 +/- 2.0 p < 0.01). The total QUIK score increased according to the severity of symptoms (WHO I 5.8 +/- 4.4, WHO II 9.3 +/- 7.2 and WHO III 12.1 +/- 5.6), respectively. The total score of WHO I was significantly lower compared with that of WHO III (p < 0.01).(ABSTRACT TRUNCATED AT 250 WORDS)

Aged↗
PubMed1978

Rat liver cysteine dioxygenase (cysteine oxidase). Further purification, characterization, and analysis of the activation and inactivation.

Rat liver cysteine dioxygenase has been purified to homogeneity. It is a single subunit protein having a molecular weight of 22,500 +/- 1,000, with a pI of 5.5. The enzyme purified was catalytically inactive and activated by anaerobic incubation with either L-cysteine or its analogues such as carboxymethyl-L-cysteine, carboxyethyl-L-cysteine, S-methyl-L-cysteine, D-cysteine, cysteamine, N-acetyl-L-cysteine, and DL-homocysteine. The enzyme thus activated with L-cysteine was rapidly inactivated under aerobic condition. This rapid inactivation was observed at 0 degrees C where no formation of either the reaction product cysteine sulfinate or the autoxidation product of cysteine, cystine, was detected. Further analysis shows that the inactivation of the activated enzyme was due to oxygen but unrelated to either the presence of substrate, enzyme turnover or accumulation of inhibitor produced during assay. A distinct rat liver cytoplasmic protein, called protein-A, could completely prevented the enzyme from the aerobic inactivation. The loss of activity during assay in the absence of protein-A was shown to be a first order decay process. From the plots of log(deltaproduct/min) versus time, the initial velocity (VO) and the velocity at 7 min (V7) were obtained. The apparent Km value for L-cysteine in the absence of protein-A was calculated from the initial velocity as 4.5 X 10(-4)M. Protein-A did not alter the apparent Km value for L-cysteine. The chelating agents such as o-phenanthroline, alpha,alpha'-dipyridyl, bathophenanthroline, 8-hydroxyquinoline, EGTA, and EDTA strongly inhibited the enzyme activity when these chelating agents were added before preactivation. The purified cystein dioxygenase contains 1 atom of iron per mol of enzyme protein. By the activation procedure, the enzyme became less susceptible to the heat denaturation, the inhibitory effects of chelating agents and the tryptic digestion.

Animals↗
PubMed1978

Decrease of rat liver cysteine dioxygenase (cysteine oxidase) activity mediated by glucagon.

The hepatic cysteine dioxygenase activity of rats was markedly decreased by the intraperitoneal administration of glucagon. The enzyme activity was also decreased by either dibutyryl cyclic AMP or theophylline. The prior administration of actinomycin D completely blocked the glucagon-mediated decrease of enzyme activity, while administrations of this inhibitor of protein synthesis after glucagon injection did not block the decrease of enzyme activity. A single administration of actinomycin D resulted in a slight increase of cysteine dioxygenase activity in the rat liver. On the other hand, the injection of cycloheximide resulted in a rapid decrease of the hepatic cysteine dioxygenase with a half-life of 2.5 h. The half-life of the enzyme in rat liver after glucagon administration was one hour. The administration of hydrocortisone or insulin had no effect on the glucagon-mediated decrease of cysteine dioxygenase of rat liver. The enzyme activity of alloxan diabetic rat liver was almost the same as that of the intact rat liver. The evidence obtained here suggests that enhancement of degradation or inactivation of cysteine dioxygenase is responsible for the glucagon-mediated decrease of the enzyme activity in rat liver.

Adrenal Glands↗
PubMed1976

Purification and some properties of rat liver cysteine oxidase (cysteine dioxygenase).

Cysteine oxidase (cysteine dioxygenase, EC 1.13.11.20) was purified approximately 1000-fold from rat liver. The purified enzyme (protein-B) was obtained as an inactive form, which was activated by anaerobic preincubation with L-cysteine. The active form of protein-B was inactivated during aerobic incubation to produce cysteine sulfinate. This inactivation of protein-B was protected by a distinct protein in rat liver cytoplasm, namely stabilizing protein (protein-A). The Ka and Km values for L-cysteine were 0.8-10(-3) M and 1.3-10(-3) M respectively. The enzyme was strongly inhibited by Cu+ and/or Fe2+ chelating agents but not by Cu2+ chelating agent. The optimum pH of enzyme reaction was 8.5-9.5 while that of enzyme activation was 6.8-9.5, with a broad peak.

Animals↗