[Check points in nursing management. Re-evaluation of work manuals used on the job].
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Biomedical subjects
Publications and source records attributed to T Takashima.
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We have carried out laboratory and clinical studies on cefteram pivoxil (CFTM-PI, T-2588). The results are summarized as follows. CFTM-PI was given through oral administration to 2 children each at dose levels of 1.5 mg/kg, 3 mg/kg and 6 mg/kg. After administration, mean peak serum levels of CFTM obtained for the 3 dose levels were 0.66 +/- 0.01 microgram/ml, 1.26 +/- 1.05 micrograms/ml and 2.28 +/- 0.95 micrograms/ml at 2 hours, respectively, and mean half-lives were 1.07 +/- 0.52 hours, 1.32 +/- 0.76 hours and 2.53 +/- 1.70 hours, respectively. Mean urinary excretion rates of CFTM were 19.0 +/- 4.0%, 9.4 +/- 1.5% and 19.9 +/- 4.0% in the first 8 hours after administration of 1.5 mg/kg, 3 mg/kg, 6 mg/kg, respectively. Treatment with CFTM-PI was made in 36 cases of pediatric bacterial infections including 20 cases of tonsillitis, 3 cases of bronchitis, 6 cases of scarlet fever, 3 cases of UTI and 1 case each of bronchopneumonia, abscess, staphylococcal scalded skin syndrome and vaginitis. Results obtained were excellent in 22 cases, good in 14 cases. No significant side effect due to the drug was observed in any cases.
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Purified bovine brain myosin contained approximately 1 and 3 mol of protein-bound phosphate/mol myosin in the light chains and heavy chains, respectively. Large portions of this light chain- and heavy chain-bound phosphate (about 0.8 and 2.4 mol, respectively) were removed by incubation with a brain phosphoprotein phosphatase and potato acid phosphatase, respectively. Upon phosphorylation of the dephosphorylated brain myosin with myosin light chain kinase and casein kinase II, about 1.6 and 3.0 mol of phosphate was incorporated into the light chains and heavy chains, respectively, while much lower levels of phosphate were incorporated into the non-dephosphorylated brain myosin under the same conditions. The actin-activated Mg2+-ATPase activity of brain myosin rephosphorylated with myosin light chain kinase was about twice as high as that of dephosphorylated brain myosin (about 30 and 15 nmol phosphate/mg/min, respectively). On the other hand, whereas the rephosphorylated brain myosin superprecipitated rapidly with F-actin, the rate of superprecipitation of the dephosphorylated brain myosin was extremely low. Under appropriate conditions, a loose network of tiny superprecipitates, which formed initially throughout the solution, contracted to form eventually a large and dense particle. These results indicate that phosphorylation of the light chains of brain myosin is a prerequisite for the contraction of brain actomyosin. The role of phosphorylation of the heavy chains by casein kinase II remains to be elucidated.
The physical properties of human platelet myosin in crude extracts were studied by means of Sepharose 4B gel filtration and sucrose density gradient centrifugation in the presence or absence of Mg-ATP. Platelet myosin extracted with a buffer containing 0-0.15 M KCl gave a Stokes radius of about 12.0-12.5 nm irrespective of the presence or absence of Mg-ATP. The sedimentation coefficients obtained in the presence of Mg-ATP were about 10-11 and 8.5S at 0.05-0.10 and 0.15 M KCl, respectively, whereas the values obtained in the absence of Mg-ATP were about 16, 9-12, and 8.5S at 0.05, 0.10, and 0.15 M KCl, respectively. The apparent molecular weight in the presence of Mg-ATP, therefore, was about 500,000 and 420,000 at 0.05-0.10 and 0.15 M KCl, respectively, while the molecular weight in the absence of Mg-ATP was about 790,000, 460,000-620,000, and 440,000 at 0.05, 0.10, and 0.15 M KCl, respectively. The purified monomeric platelet myosin that had been solubilized with Mg-ATP at 0.10 M KCl had a Stokes radius of about 12.5 nm, a sedimentation coefficient of about 9S, and an apparent molecular weight of 460,000. On the other hand, while crude platelet myosin extracted at 0.6 M KCl with Mg-ATP gave a Stokes radius of about 20 nm, a sedimentation coefficient of about of 6S, and an apparent molecular weight of about 490,000, each of these physical parameters obtained in the absence of Mg-ATP was much larger than that obtained in the presence of Mg-ATP because the myosin was associated with F-actin.(ABSTRACT TRUNCATED AT 250 WORDS)
Growth of mouse-virulent Mycobacterium intracellulare D673 and TMC 1405 in the lung was affected by T-cell depletion in susceptible C57BL/6 mice. Significant differences also occurred between the growth patterns seen in congenitally athymic (nu/nu) mice and their nu/+ littermates. Treatment of the mice with an immunosuppressive regimen of cyclosporin A (75 mg/kg of body weight per day subcutaneously) provided further evidence of the importance of T cells in controlling growth of M. intracellulare in the normal host. Adoptive transfer experiments indicated the presence of a T-cell-mediated specific protective immunity against a subsequent M. intracellulare challenge when transfer was carried out 3 weeks after immunization of the donor host. At this time, cross-protective immunity was also observed against a virulent M. tuberculosis challenge. There was no difference in the rate of growth by M. intracellulare as challenge in Mycobacterium bovis BCG-activated or normal peritoneal macrophages from C57BL/6 mice tested in vitro during a 7-day period. However, M. tuberculosis growth rates were decreased substantially in the BCG-activated macrophages. These studies suggest that mice infected with M. intracellulare do not eliminate the infection, because this organism can resist the bactericidal activity of the T-cell-activated macrophage better than M. tuberculosis can.
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We describe the sonographic, CT and angiographic findings in 10 cases of hepatocellular carcinoma in which extensive fatty metamorphosis occurred within the tumors. Fatty change was diffuse in smaller tumors (less than 3.5 cm) and focal in larger tumors (greater than 3.5 cm). Fatty metamorphosis characteristically caused a low-attenuation area on CT (less than -10 H) and a highly echogenic area on sonography. The sonographic appearance of small hepatocellular carcinomas with fatty metamorphosis was identical to the findings in cavernous hemangioma or focal fatty change of the liver. CT correctly revealed the presence of fat in these hepatocellular carcinomas. In these cases, hepatic arteriography showed no tumor stain; however, CT arteriography (dynamic CT during injection of contrast medium into the hepatic artery) was useful in showing the tumor, its capsule, and its internal septa. In the diagnosis of large hepatocellular carcinoma, the presence of intratumoral fat is not likely to be problematic, but small tumors that are diffusely infiltrated by fat must be distinguished from such benign conditions as focal fatty change, lipoma, and angiomyolipoma.
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Many nasal sprays used in the treatment of rhinitis contain a steroidal agent, giving rise to fear of side effects when they are used frequently and continually. Accordingly, we undertook the development of a nasal spray containing oxaprozin, a nonsteroidal anti-inflammatory agent. Suitable discharge pressure and surfactants were determined by applying trial aerosols to human subjects in "feeling" tests to assess approval rating. Other tests showed that about 80% of the expelled oxaprozin was released into the nasal cavity, and that the chosen formulation caused only a low level of irritation to the nasal mucosa. Most of the aerosol particles were found to adhere to Kiesselbach's area and the frontal region of the inferior concha, which are the major areas where inflammation and nasal haemorrhage occur. When the nasal spray was administered to 50 patients, a sufficient therapeutic effect was achieved, especially in the treatment of nasal haemorrhage, and side effects have not yet been detected.
Pharmacokinetic and clinical studies on ceftriaxone (CTRX) in mature and premature neonates were carried out. The results are summarized as follows. The mean serum peak level of CTRX after intravenous administration at a single dose of 10 mg/kg in 4 to 13 day-old-neonates was 34.1 +/- 11.4 micrograms/ml at 30 minutes. The mean serum level at 12 hours after dosage was 11.1 +/- 2.1 micrograms/ml. The mean half-life time was 11.6 +/- 1.4 hours. Mean serum peak levels of CTRX after intravenous administration at a single dose of 20 mg/kg were 64.6 +/- 15.4 micrograms/ml in 1 to 3 day-old-neonates, 44.6 +/- 1.1 micrograms/ml in 5 day-old-neonates at 30 minutes. Mean serum levels at 12 hours after dosage in these two groups of neonates were 16.4 +/- 4.8 micrograms/ml and 12.4 +/- 2.5 micrograms/ml, respectively. Mean half-life times were 13.7 +/- 3.7 hours in 1 to 3 day-old-neonates and 10.2 +/- 1.3 hours in 5 day-old-neonates. CTRX was clinically effective in a case of urinary tract infection. No side effect was observed except an elevation of GOT.
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