[Nursing process: nursing process of patients with stomach cancer. Evaluation of the nursing process. Discussion].
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Biomedical subjects
Publications and source records attributed to N Okada.
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Transfer ribonucleic acid (tRNA) guanine transglycosylase (guanine insertion enzyme) was isolated from rat liver and extensively purified. The enzyme catalyzes an exchange of queuine (the base of queuosine, Q) as well as its precursors and guanine for guanine originally located in the first position of the anticodon of "undermodified" tRNATyr, tRNAHis, tRNAAsn, and tRNAAsp from an Escherichia coli mutant or rat ascites hepatoma cells. This is in contrast to the previous observation that E. coli tRNA-guanine transglycosylase catalyzes the exchange of queuine precursors, such as 7-(aminoethyl)-7-deazaguanine and 7-cyano-7-deazaguanine, but not of queuine itself [Okada, N., Noguchi, S. Kasai, H., Shindo-Okada, N., Ohgi, T., Goto, T., & Nishimura, S. (1979) J. Biol. Chem. 254, 3067-3073]. The Km value for queuine of the rat liver enzyme is 9.2 X 10(-7) M, much lower than the values for the bases of queuosine precursors or guanine. Thus, the actual substrate for tRNA-guanine transglycosylase in queuosine biosynthesis in vivo in rat liver may not be 7-(aminomethyl)-7-deazaguanine, which is thought to be an actual substrate guanine, the E. coli system. Queuine or some queuine derivative may be the actual substrate for the tRNA-guanine transglycosylase reaction in the biosynthesis of Q in tRNA of mammalian cells. 6-Thioguanine and 8-azaguanine are also found to be good substrates.
Human keratinocytes in culture were treated with dibutyryl cyclic AMP (DBcAMP) at concentrations of 10(-3) and 10(-4) M, and labeled with [3H]histidine for 48 hours. The proteins of the keratinocytes were serially extracted in 0.25 M sucrose, 0.1 M sodium citrate-citric acid (pH 2.6), 6 M urea-0.1 M Tris-HCl(pH 9.0), and 6 M urea-0.1 M Tris-HCl(pH 9.0) with 1% mercaptoethanol. The incorporation of [3H]histidine into the extract as assayed by DPM of 3H/microgram protein was increased in 0.25 M sucrose extract and Tris-urea extract of the cultures treated with 10(-3) M and 10(-4) M DBcAMP as compared with the control culture. There was no difference between the citrate-buffer extract of the control and that of the DBcAMP-treated cultures. The incorporation of [3H]histidine into the Tris-urea-mercaptoethanol extract was small, and this fraction was thought to be inactive metabolically. It was concluded that dibutyryl cycli AMP stimulated the protein synthesis of the cultured keratinocytes and induced a qualitative change toward accelerating the synthesis of keratinous protein.
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Since 1973, the balloon catheter test with a Swan-Ganz, Dotter-Lukas or Fogarty catheter has been attempted in our department in cases of atrial septal defect (ASD) and patent ductus arteriosus (PDA) during cardiac catheterization and operation. Accurate informations concerning size, number and location of ASD were obtained during cardiac catheterization studies by using the balloon catheter. The difference between the size of the defect measured at catheterization and at operation was less than 1 mm in diameter. Size of the defect ranged from 13 to 44 mm in diameter (25.7 mm on the average) and bacame larger with patient's age. Measurement of left-to-right shunt ratios before and after the temporary balloon occlusion of the defect was of help in making a preoperative diagnosis of ASD with multiple defects. Size of foramen ovale ranged from 3 to 13 mm in diameter (5.2 mm on the average) and was not related to age. Size of the ductus in cases with PDA was measured during cardiac catheterization by using the balloon catheter. The difference between the size of the ductus measured with the balloon technique at catheterization and with a measuring rule at operation was less than 4 mm in diameter. The difference revealed the extensibility of the ductus. The temporary balloon occlusion of the ductus aided in determining presence of other cardiac anomalies. In cases of isolated PDA, the murmur became inaudible with the occlusion of the ductus. A balloon catheter inflated with radiopaque dye was used for measurements at cardiac catheterization and at operation. Persistent arrhythmias or other adverse effects of this procedure were not observed.
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A guanine insertion enzyme (tRNA transglycosylase) was purified to a homogeneous state from Escherichia coli B by ammonium sulfate fractionation and DEAE-cellulose, DEAE-Sephadex A-50, phosphocellulose, and Sephadex G-200 column chromatographies. The molecular weight of the enzyme, which appeared to be a single polypeptide, was 4.6 X 10(4) by sodium dodecyl sulfate gel electrophoresis. The enzyme catalyzes exchange of guanine with guanine located in the first position of the anticodon of tRNATyr, tRNAHis, tRNAAsn, and tRNAAsp, but unlike the enzymes isolated from rabbit reticulocytes and Ehrlich ascites tumor cells it does not catalyze the exchange of guanine with queuine (7-(3,4-trans-4,5-cis-dihydroxy-1-cyclopenten-3-ylaminomethyl)-7-deazaguanine) present in these tRNAs. The pH optimum of the reaction was 7.0, and the pH1 value was 4.6 to 4.8. The reaction required Mg2+ ion. 7-Methylguanine inhibited guanine insertion, but the other purine analogues tested were not inhibitory and could not replace guanine.20
The guanine insertion enzyme isolated from Escherichia coli (tRNA transglycosylase) catalyzed the incorporation of bases of Q (queuosine) precursors into E. coli undermodified tRNAAsn and tRNATyr. These bases of Q precursors were inserted in the first position of the anticodon of tRNASn and tRNATyr, replacing guanine originally located in that position. This is a novel type of post-transcriptional modification, inserting a modified base into the polynucleotide chain by cleavage of the N--C glycoside bond without breakage of the phosphodiester bond. One of the bases of Q precursors, 7-(aminomethyl)-7-deazaguanine, was found in the acid-soluble fraction of E. coli cells, supporting the conclusion that formation of Q, 7-(3,4-trans-4,5-cis-dihydroxy-1-cyclopenten-3-ylaminomethyl)-7-deazaguanosine, in tRNA in vivo actually proceeds by the tRNA transglycosylase reaction.
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FK 749 is a new parenteral cephalosporin derivative which is more active against various gram-negative bacilli, including the opportunistic pathogens such as Enterobacter, Citrobacter species, and Serratia marcescens, than cephalosporins and cephamycins such as cefotiam, cefamandole, cefuroxime, cefotaxime, and cefmetazole. FK 749 was especially active against gram-negative organisms resistant to these related antibiotics. FK 749 was more potent in bactericidal activity than the other antibiotics, and the activity was clearly enhanced in the presence of 90% defibrinated rabbit blood. The therapeutic effect of subcutaneously injected FK 749 in mice infected with various gram-negative bacilli was far superior to that of cefotiam, cefamandole, cefuroxime, and cefmetazole and was almost the same as that of cefmetazole in mice infected with Staphylococcus aureus and that of ticarcillin in mice infected with Pseudomonas aeruginosa. FK 749 has, in general, nearly the same in vitro and in vivo antibacterial activities as cefotaxime. The former had more potent bactericidal activity in the presence of the blood than the latter and showed more excellent therapeutic effect than cefotaxime against infections caused by large inoculum sizes.
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FK 749 is a distinctive new parenteral cephalosporin antibiotic with a broad antibacterial spectrum which is more potently active against a wide variety of Gram-negative bacilli, including the opportunistic pathogens such as Citrobacter and Enterobacter species and Serratia marcescens, than SCE 963, T 1551 and cefmetazole. The activity of FK 749 against Escherichia coli, Klebsiella pneumoniae, pyogenes was by far superior to that of the three other antibiotics. These test organisms were not resistant to FK 749. The antibacterial activity of FK 749 against Pseudomonas aeruginosa was almost the same as that of ticarcillin but was inferior to that of gentamicin and T 1551. The bactericidal activity of FK 749 against E. coli, K. pneumoniae and Proteus mirabilis was more potent than that of the three other antibiotics. FK 749, like cefmetazole, was extremely stable to beta-lactamases. In studies in mice, the therapeutic effect of subcutaneous injection of FK 749 against various infections due to Gram-negative bacilli was by far superior to that of SCE 963, T 1551 and cefmetazole, was almost the same as that of SCE 963 and cefmetazole against Staphylococcus aureus infection and that of ticarcillin against P. aeruginosa infection.
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