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Biomedical subjects

I Kato

Publications and source records attributed to I Kato.

At least 649 records · Page 36Linked to original sources
PubMed1979

Response of urinary noradrenaline excretion to reserpine administration in normal and hypertensive subjects.

Reserpine was administered in purpose to determine the "Noradrenaline store" in sympathetic nerve endings. The marked increase of urinary noradrenaline excretion was observed by reserpine 0.4 mg/day administration. Total amount of noradrenaline in urine for first three days of 0.4 mg/day of reserpine administration was considered as a good indicators of "Noradrenaline store". There was no difference of "Noradrenaline store" between normal and hypertensive subjects. The increase % of urinary noradrenaline was higher in labile hypertension than in established hypertension as well as in normal subjects. Though the relationship between "Noradrenaline store" or the increase % of noradrenaline and sympathetic nerve activity was not clear, it is suspected that the releasable noradrenaline in sympathetic nerve granule was higher in labile hypertension than in established hypertension or normal subjects.

Adult↗
PubMed1979

Caloric pattern test with special reference to failure of fixation-suppression.

Fixation-suppression of caloric nystagmus was studied in 1230 consecutive cases. An analysis of caloric nystagmus with failure of fixation-suppression (FFS) made it possible to classify patterns of FFS into three types: Type I: FFS was observed bilaterally in caloric nystagmus; Type II: FFS was recognized unilaterally on either side; Type III: FFS was seen in either direction of nystagmus. On the basis of these three types, the underlying neuroanatomical substrate responsible for FFS is discussed.

Brain Diseases↗
PubMed1979

Surface glycopeptide change triggered by contact between normal cells from rat liver and their simian virus 40-transformed cells from the same virus.

Surface glycopeptide changes triggered by mixed culture of normal cells from rat liver cell line WIRL-3 and simian virus 40-transformed cells from the same line were studied. In addition, biologic responses of the normal cells and the transformed cells to three kinds of surface glycopeptides derived from the normal cells, the transformed cells, and these cells in mixed culture were investigated. Surface glycopeptide derived from the mixed culture showed a quantitative increase and a qualitative change in the glycopeptide structure, not detected in the surface glycopeptide of normal cells and transformed cells cultured separately. The surface glycopeptide changes observed in the mixed culture were mainly ascribable to normal cells responding to transformed cells, and a surface glycopeptide change in normal cells induced a qualitative surface glycopeptide change in transformed cells. Differences in biologic response of normal cells and transformed cells to the above three surface glycopeptides were investigated with the use of inhibition of [3H]thymidine uptake of the cells by the three different surface glycopeptide preparations. The inhibition rates of uptake in normal cells were 30% by all three surface glycopeptides (200 microgram/ml culture medium); inhibition rates in transformed cells were 65% by mixed-culture surface glycopeptide, 50% by normal cell-surface glycopeptide, and 35% by transformed cell-surface glycopeptide.

Cell Communication↗
PubMed1979

Neurotological studies on Meniere's disease and sudden deafness.

During the period from January 1973 to June 1975, 60 cases with definite Meniere's disease and 30 cases with sudden deafness were listed according to such criteria for the diagnosis of both diseases as determined by the Research Committee of Japan. A neurootological assessment for both diseases were performed in our series. In patients with definite Meniere's disease, hearing impairment was characterized by deficiency in detecting low- and middle-pitched tones and fluctuation of auditory threshold in low frequency range. In sudden deafness, highly impaired hearing loss, i.e., total deafness, was frequently observed (45%). However, recruitment occurred at the same incidence (80%) in both diseases tested. The incidence of spontaneous nystagmus was almost the same regardless of associated vertigo and the course of both diseases. Moreover, it was also recognized that a reduction of caloric responses was a better indication for assessment of the affected ear in both diseases.

Audiometry↗
PubMed1978

Angiotensin I-converting enzyme in human urine.

It was demonstrated that angiotensin I-converting enzyme was excreted in human urine. The mean activity of the enzyme in normal urine was found to be 0.38 +/- 0.04 (S.E.M.) units/day (n = 18) and the enzymic activity correlated well with the concentration of the excreted sodium (r = 0.76, p less than 0.005). Urinary angiotensin I-converting enzyme was partially purified. Three different molecular weights of enzyme (greater than 400 000, 290 000 and 140 000) were demonstrated by Sephadex G-200 gel filtration. The enzymic properties of these three enzymes were identical with those of angiotensin I-converting enzyme from human lung with regard to inhibitory effects (bradykinin potentiator c and Arg-Pro-Pro), Cl- dependency, pH optimum and KM value.

Angiotensin-Converting Enzyme Inhibitors↗
PubMed1978

Purification and some properties of a lethal toxic fragment of staphylococcal alpha-toxin by tryptic digestion.

Purified staphylococcal alpha-toxin (molecular weight approximately 36,000) was mildly digested with trypsin, yielding two components by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A fast-moving component (molecular weight 17,000 +/- 5%) which is relatively resistant to tryptic digestion and a slow-moving component (molecular weight 20,000 +/- 5%) which tends to aggregate. The fast-moving component was highly purified by means of combined procedures of column chromatography on Sephadex G-200 with zone electrophoresis on starch. The purified fast-moving component retained a high degree of lethal toxicity for mouse but lacked hemolytic and dermonecrotic activities, whereas the slow-moving component proved to be a nontoxic polypeptide. The lethal toxic fragment was antigenically active showing partial immunological identity with the parent alpha-toxin and stimulated the formation of antibodies capable of neutralizing the lethal action of alpha-toxin in vivo. Some physical properties and the amino acid composition of the purified lethal toxic fragment have been compared with those of native alpha-toxin.

Animals↗