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Biomedical subjects

N Horie

Publications and source records attributed to N Horie.

At least 91 records · Page 5Linked to original sources
PubMed1988

A novel lysine-substituted nucleoside in the first position of the anticodon of minor isoleucine tRNA from Escherichia coli.

A minor species of isoleucine tRNA (tRNA(minor Ile)) specific to the codon AUA has been isolated from Escherichia coli B and a modified nucleoside N+ has been found in the first position of the anticodon (Harada, F., and Nishimura, S. (1974) Biochemistry 13, 300-307). In the present study, tRNA(minor Ile)) was purified from E. coli A19, and nucleoside N+ was prepared, by high-performance liquid chromatography, in an amount (0.6) A260 units) sufficient for the determination of chemical structures. By 400 MHz 1H NMR analysis, nucleoside N+ was found to have a pyrimidine moiety and a lysine moiety, the epsilon amino group of which was involved in the linkage between these two moieties. From the NMR analysis together with mass spectrometry, the structure of nucleoside N+ was determined as 4-amino-2-(N6-lysino)-1-(beta-D-ribofuranosyl)pyrimidinium ("lysidine"), which was confirmed by chemical synthesis. Lysidine is a novel type of modified cytidine with a lysine moiety and has one positive charge. Probably because of such a unique structure, lysidine in the first position of anticodon recognizes adenosine but not guanosine in the third position of codon.

Anticodon↗
PubMed1986

Proteolytic enzymes in human eccrine sweat: a screening study.

Thermally induced human eccrine sweat was collected both by simple scraping (SS) and by a polyethylene sweat collector that covered the Vaseline-coated skin of the back to minimize epidermal contamination (CS, clean sweat). Using synthetic chromogenic Kabi S-series substrates, we demonstrated a variety of proteases in both SS and CS, the former being higher than the latter to varying extents. The higher enzyme activity in SS is mainly due to epidermal contamination because abundant protease activity was eluted from the nonperspiring stripped and unstripped skin in vivo and from the stripped stratum corneum itself. The electrophoretic separation of sweat protein has shown that CS contains at least 7 and SS 15 gelatinolytic proteinases. Although some CS proteinases could be derived from the sweat duct, the sweat secretory coil itself is responsible for at least two proteinases at 78 and 25 kilodaltons. The identity and function of these enzymes remain to be studied.

Caseins↗
PubMed1985

Two tRNAIle1 species from an extreme thermophile, Thermus thermophilus HB8: effect of 2-thiolation of ribothymidine on the thermostability of tRNA.

From Thermus thermophilus HB8 grown at 65 degrees C, two major tRNAIle species have been purified by column chromatography and polyacrylamide gel electrophoresis. The nucleotide sequence of one of these two tRNAIle1 species (tRNAIle1a) has been determined to be pGGGCGAUUAGCUCAGCUGmGUDAGAGCGCACGCCUGAUt6AAGCGUGAGm7GUCGGUGGs2T psi CAm1AGUCCACCAUCGCCCACCAOH. The nucleotide sequence of the other species (tRNAIle1b) is found to be the same as that of tRNAIle1a except for the modification in position 54; tRNAIle1a has s2T(54) while tRNAIle1b has T(54). The melting temperature of tRNAIle1a is as high as 86.2 degrees C while that of tRNAIle1b is 83.3 degrees C. The single replacement of an oxygen atom (2-carbonyl oxygen) of T(54) by a sulfur atom significantly contributes to the thermostability of the tRNAIle1a species. In addition, the methylation of G(18) and A(58) possibly contributes to the thermostability of T. thermophilus tRNAIle1a and tRNAIle1b species.

Base Sequence↗
PubMed1985

Variation in activities of non-plasmin fibrinolytic proteinase and plasminogen-activator in the lung and spleen induced by bacterial endotoxin in rats with special reference to the effects of MD-805.

The behavior of direct fibrinolytic (non-plasmin) proteinase activity and plasminogen-activator activity in the lung and spleen was investigated in rats after a single intravenous injection of bacterial endotoxin, and the influence of thrombin inhibitors on the effects of the endotoxin was assessed. The non-plasmin fibrinolytic activity was markedly increased following a decrease of plasminogen-activator in the lung. In addition, variations in hematological parameters, i.e. a decrease of platelet count, fibrinogen level and antithrombin III, and an increase of blood urea nitrogen and euglobulin fibrinolytic activity, were induced by the injection, indicating the occurrence of disseminated intravascular coagulation. In comparative studies on the effects of the endotoxin injection and thrombin infusion, in the lung and spleen an increase of fibrinolytic proteinase activity was induced in a similar manner; the plasminogen-activator activity in the lung was decreased by the endotoxin injection but not decreased by the thrombin infusion. In prevention studies with heparin and MD-805, the latter was found to prevent the decrease of either fibrinogen or platelet count. However, the former failed to prevent the decrease of platelet count although that of the fibrinogen level was prevented. Heparin and MD-805 exerted no preventive effect on the endotoxin-induced variations of proteinase activity and plasminogen-activator activity in the lung.

Animals↗
PubMed1985

[Clinical evaluation of lenampicillin in the treatment of superficial suppurative skin and soft tissue infection. A double-blind study comparing amoxicillin].

A double-blind controlled clinical study between lenampicillin (LAPC), a newly developed oral ampicillin (ABPC) prodrug, and amoxicillin (AMPC) was conducted for the treatment of suppurative skin and soft tissue infection as grouped in 6 disease types. LAPC or AMPC were orally administered at a daily dose of 1,000 mg, in 4 equally divided doses. Each group was treated for 14 days. The results indicated that LAPC was equal to AMPC in evaluations of effectiveness and usefulness, although incidence of severe side effects was slightly lower in LAPC. The number of cases studied was 235 (115 in the LAPC group, 120 in the AMPC group). Among these, 10 patients (4 in LAPC, 6 in AMPC) were excluded and 12 patients (5 in LAPC, 7 in AMPC) dropped out. Final global improvement rating was evaluated in 213 patients (106 in LAPC, 107 in AMPC). General usefulness rating was evaluated in 215 patients (106 in LAPC, 109 in AMPC), and overall safety rating was evaluated in 231 patients (115 in LAPC, 116 in AMPC). Final global improvement rating of LAPC was, "cured", 55.7% and "cured" and "remarkably improved", 79.2%. The rate increased to 88.7% when "improved" was included. On the other hand, in the AMPC group, "cured" was 50.5%, and "cured" and "remarkably improved" was 76.6%. The rate increased to 91.6% when "improved" was included. No significant difference was found between the 2 drug groups. In overall safety rating of LAPC, "safe" was 93.9%, while in the AMPC group, "safe" was 94.0%. No significant difference was found between the 2 drug groups. Side effects were noted in 2 of 115 patients (1.7%) among the LAPC group and in 5 of 116 patients (4.3%) among the AMPC group. Incidence of severe side effects was slightly lower in LAPC (P less than 0.1). General usefulness rating of LAPC was, "remarkably useful", 56.6% and the rate increased to 86.8% when "useful" was included. In the AMPC group, "remarkably useful" was 51.4%, and increased to 84.4% when "useful" was included. No significant difference was found between the 2 drug groups.

Adult↗
PubMed1985

[Clinical studies on lenampicillin in the therapy of skin and soft tissue infections].

Clinical evaluation of newly developed oral ampicillin prodrug lenampicillin (LAPC, KBT-1585) applied to patients with superficial purulent infection at a dosage of 750 approximately 1,500 mg daily was conducted. Additionally, as part of the basic study, transition of the compound to the human skin tissue was observed. With regard to transition to human skin tissue in 11 presurgery dermatitis cases, 250 mg or 500 mg of LAPC was administered to 2 approximately 3 hours before surgery. Comparison was made between concentrations in serum and in skin tissue. Results in the case of 250 mg application showed serum concentration to be 1.28 approximately 3.32 micrograms/ml, and in skin tissue, 0.13 approximately 0.82 micrograms/g. At 500 mg, serum concentration was found to be 2.23 approximately 10.05 micrograms/ml, with skin tissue concentration at 0.45 approximately 1.34 micrograms/g. Rate of clinical efficacy in the treatment of the 183 cases of superficial purulent infection was 79.2%. By grouping of the infections (Table 3), high efficacy rates were obtained in the second group, at 85.7%; in the third at 88.9%; and in the fourth group at 96.4%. Evaluation of usefulness from the standpoint of safety was 77.6%. Good results were obtained in the third group with 88.9%; and in the fourth group with 96.4%. LAPC's efficacy rates against individual strains of bacteria in simple infection are as follows: Staphylococcus aureus, 74.6%; Staphylococcus epidermidis, 76.3%; GPC, 100%; anaerobes, 87.5%. In polymicrobial infections the rate was 84.6%. The rate of efficacy against all strains of bacteria was 76.0%. Adverse reactions were found in 13 cases (14 incidences) out of 193. The rate of incidence was 7.3%, with allergic response accounting for 5 cases, digestive tract disorders, 7 cases, and mouth odor, 1 case. There were 5 cases (6 incidences) of abnormal deviation of laboratory findings. In all cases, abnormal deviations were mild and their relation to the drug was unclear.

Administration, Oral↗
PubMed1984

Enzymatic activity of metal-binding proteins in epidermal cells.

Enzymatic activity was investigated in metal-binding proteins from rat epidermal cells. Tris-HCl buffer soluble and KSCN solubilized proteins were extracted stepwise from granular and cornified cells of 2-day old rat epidermis. Each extract was separately applied to a Cu2+ or Zn2+ chelate Sepharose 6B column and the proteins were eluted with buffers of different pHs and finally with EDTA solution. Metal chelate-binding proteins were found in both soluble and solubilized proteins but there was a larger amount in the latter. Affinity of the proteins to bind with Cu2+ chelate was greater than that with Zn2+ chelate. In Tris-HCl buffer extract, histidase activity was detected in Cu2+ chelate-binding proteins, but not in Zn2+ chelate-binding proteins. Acid phosphatase, cysteine proteinase, dipeptidase, cathepsin D, beta-galactosidase, gelatin hydrolase, and superoxide dismutase did not bind to metal chelates although these enzymes, except acid phosphatase, were inhibited by Cu2+, but not by Zn2+. In contrast, KSCN solubilized metal chelate-binding proteins showed plasminogen activator, acid phosphatase, and gelatin and casein hydrolases while histone hydrolase did not bind to either chelate column. Since metal-binding proteins in rat epidermal cells have been shown previously to be histidine- and cysteine-rich proteins concentrated in keratohyalin granules, interaction of metals and the structural proteins with certain enzymes may be involved in the regulation of epidermal cell functions.

Animals↗
PubMed1984

Detection and characterization of epidermal proteinases by polyacrylamide gel electrophoresis.

Electrophoresis of cornified cell extracts of 2-day-old rats, using SDS polyacrylamide gels copolymerized with alpha-casein or gelatin with or without plasminogen, was performed. Both Tris-HCl buffer soluble protein and KSCN solubilized protein contained a number of hydrolases for alpha-casein and/or gelatin, but PA (mol. wts 57 and 50K) was found only in the KSCN extract. The pH dependency, substrate specificity and mol. wt of plasminogen-independent proteinases were comparatively determined and DFP inhibition tested. This simple technique helped to identify the presence of several proteinases and to characterize them in partially purified epidermal extracts.

Animals↗
PubMed1981

Plasminogen-activator in human early milk: its partial purification and characterization.

Milk plasminogen-activator was partially purified from human transitional milk collected at about 10 days after delivery, by a five-step procedure involving chloroform treatment, ammonium sulfate precipitation, and column chromatography on Sephadex G-150, CM Sephadex C-50 and DEAE Sephadex A-50. This gave milk-activator with a maximum purification factor of about 2,400-fold with respect to the skimmed milk. The CM Sephadex-step preparation showed, on polyacrylamide gel electrophoresis, a single plasminogen-activator activity band located between the bands of albumin and prealbumin of human serum. This preparation exhibited no kinin forming activity. The activator hydrolyzed acetyl-glycyl-L-lysine methyl ester with similar order kinetic constants to urokinase, and was inhibited strongly by diisopropylfluorophosphate. The molecular weight of the activator as estimated by gel filtration was approximately 86,000, the isoelectric points as estimated by gel isoelectric focusing were pH 7.2, 6.9 and 6.6, and the activator activity was not quenched by antiurokinase globulin, indicating that the milk-activator is a different entity from urokinase.

Ammonium Sulfate↗