[Problems observed with ovarian cancer patients].
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Female↗
Biomedical subjects
Y Fukagawa
Publications and source records attributed to Y Fukagawa.
Microbial phosphorylation of the OA-6129 group of carbapenem compounds.
The OA-6129 group of carbapenem antibiotics were phosphorylated with ATP by Brevibacterium ammoniagenes at the primary hydroxyl group of the C-3 pantetheinyl side chain. The phosphorylation resulted in the reduced antimicrobial activity against some Gram-positive bacteria, and the improved activity against some Gram-negative microbes. The increased resistance of the OA-6129 carbapenems due to phosphorylation was significant to mouse renal dehydropeptidase and moderate to the human enzyme. OA-6129A and B2 phosphates were found to be unsusceptible to A933 acylase, while OA-6129A and B2 were depantothenylated.
Bacteria↗
Studies on the biosynthesis of carbapenem antibiotics. III. Enzymological characterization of the L-amino acid acylase activity of A933 acylase.
A933 acylase, which is involved in exchange of the pantothenyl substituent of OA-6129 carbapenems with acetyl CoA, was characterized as an L-amino acid acylase with a molecular weight of 100,000 (+/- 8,000) and a pI value of 5.1. The highest L-amino acid acylase activity of A933 acylase was observed at 37 degrees C and pH 7 approximately 7.5 for N-chloroacetyl-L-phenylalanine. Unlike other amino acid acylases, A933 acylase was severely inhibited by cobalt ions and p-chloromercuribenzoate. The acylase also showed peptidase activity with some di- and tripeptides. A protein fraction with A933 L-amino acid acylase activity from blocked mutant 1501 lacked OA-6129A-depantothenylating activity.
Amidohydrolases↗
Studies on the biosynthesis of carbapenem antibiotics. IV. Beta-alanine in the C-3 pantetheinyl side chain of the OA-6129 group of carbapenems.
Radioactive beta-alanine was specifically incorporated into the beta-alanine moiety of the C-3 pantetheinyl side chain of the OA-6129 group of carbapenems by Streptomyces sp. OA-6129, while no added radioactive pantothenate was taken up into the mycelia. The extracellular concentrations of beta-alanine and pantothenate in the broth of Streptomyces sp. OA-6129 increased with the production of the carbapenems. The production levels of beta-alanine and pantothenate markedly differed between carbapenem-producing streptomycetes and nonproducers, with the exception of Streptomyces cattleya, a thienamycin producer, suggesting a possible relation of carbapenem biosynthesis with the levels of beta-alanine and pantothenate.
Alanine↗
[A history of nursing in Fukuoka Prefecture].
Nurses who had learned the Nightingale's nursing method in the middle of the Meiji Era systematized nursing in Japan. In 1884, modern nursing began in Tokyo. In Kyushu, nursing education started in Fukuoka Hospital ten years later. At that time, the teaching of nurses was done by individual doctors who taught them all the necessary subjects. This study identifies the ethical criteria which the educators of that time had as the goal of nursing education.
Curriculum↗
Deepoxidation of 16-membered epoxyenone macrolide antibiotics. I. Microbial deepoxidation and subsequent isomerization of deltamycins A1, A2, A3, A4 (carbomycin A) and X.
Carbomycin A (deltamycin A4) was deepoxidized to carbomycin A P1 by Streptomyces halstedii subsp. deltae (a deltamycins producer), favorably under anaerobic conditions. Carbomycin A P1 was spontaneously converted to geometric isomers designated carbomycins A P2 and A P3. This type of deepoxidation and subsequent isomerization was not limited to carbomycin A, but generally occurrable in other 16-membered epoxyenone macrolide compounds. Many bacteria and actinomycetes were also found to have an ability to deepoxidize deltamycins reductively. The chemical structures of carbomycins A P1, A P2 and A P3 were elucidated as shown in Fig. 3.
Bacteria↗
Deepoxidation of 16-membered epoxyenone macrolide antibiotics. II. Chemical deepoxidation by dissolving metal reduction.
16-Membered epoxyenone macrolide antibiotics were reductively deepoxidized with dissolving metals such as zinc. Angolamycin and rosamicin which have a methyl substituent at C-12 in the epoxyenone structure were deepoxidized, but not isomerized further to the geometric isomers P2 and P3.
Anti-Bacterial Agents↗
Deepoxidation of 16-membered epoxyenone macrolide antibiotics. III. In vitro and in vivo evaluation of deepoxidation products of carbomycin A, deltamycin A1, 4"-phenylacetyldeltamycin, angolamycin and rosamicin.
Deepoxidation products P1, P2 and P3 of carbomycin A, deltamycin A1 and 4"-phenylacetyldeltamycin showed high in vitro antibacterial and antimycoplasmal activities which were comparable to those of the respective parent compounds. By contrast, the in vitro antimicrobial potencies of angolamycin P1 and rosamicin P1 were about ten-fold lower than those of the parent macrolides. In mice, the increase in the plasma levels of the epoxyenone macrolides due to deepoxidation was highly significant with the P1, P2 and P3 derivatives of carbomycin A and 4"-phenylacetyldeltamycin, whereas angolamycin P1 gave a moderately-improved plasma level compared with angolamycin.
Animals↗
Studies on the biosynthesis of carbapenem antibiotics. I. Biosynthetic significance of the OA-6129 group of carbapenem compounds as the direct precursors for PS-5, epithienamycins A and C and MM 17880.
Based on the working hypothesis that the OA-6129 group of carbapenem compounds might be the direct precursors for PS-5, epithienamycins A and C and MM 17880, Streptomyces fulvoviridis A933 17M9, a producer of PS-5, PS-6, PS-7, PS-8, epithienamycins A, B, C and D, MM 17880, MM 13902 and MM 4550, was subjected to NTG-mutation to provide a blocked mutant numbered 1501 which was found to produce OA-6129 A, OA-6129B1, OA-6129B2 and OA-6129C instead of PS-5, epithienamycins A and C and MM 17880, respectively. In a cell-free system, the parent strain demonstrated an ability to convert OA-6129A to NS-5, whereas the mutant did not. The L- and D-amino acid acylases were also shown to depantothenylate the OA-6129 group of carbapenems.
Amidohydrolases↗
Studies on the biosynthesis of carbapenem antibiotics. II. Isolation and functions of a specific acylase involved in the depantothenylation of the OA-6129 compounds.
A specific acylase designated A933 acylase was isolated and purified to 90% protein homogeneity from Streptomyces fulvoviridis A933 17M9 which produces PS-5, epithienamycins A and C and MM 17880 together with minor carbapenem analogs, penicillin N and cephamycin C. This enzyme was found to catalyze the depantothenylation of OA-6129 carbapenems; the acyl exchange of OA-6129 carbapenems with acyl CoA's; the deacetylation of N-acetyl-L-amino acids; and the acylation of NS-5 and 6-aminopenicillanate with acyl CoA's, whereas the deacetylation of PS-5 and N-acetyl-D-amino acids; and the deacylation of benzylpenicillin and cephalosporin C were not observed. Similar enzyme activities were also detected in Streptomyces cattleya, Streptomyces cremeus subsp. auratilis and Streptomyces argenteolus which are all carbapenem producers.
Acyl Coenzyme A↗
Synergism of PS-5 with penicillins and cephalosporins in antimicrobial activity against beta-lactam-resistant gram-negative microorganisms.
The in vitro synergism of PS-5 combined with various penicillins and cephalosporins in antimicrobial activity was examined in detail against beta-lactam-resistant Gram-negative bacteria. PS-5 showed a highly significant synergism in antimicrobial action against Escherichia coli RGN238 in combination with penicillins; and against Proteus vulgaris GN76 and Serratia marcescens T55 in combination with cephalosporins. It was moderately synergistic against Citrobacter freundii GN346, Enterobacter cloacae 45, Proteus morganii 111 and Enterobacter aerogenes E19, whereas no synergism was observed against Pseudomonas aeruginosa E2 and Klebsiella pneumoniae 130.
Anti-Bacterial Agents↗
Structures of OA-6129D and E, new carbapenam antibiotics.
The structures and stereochemistry of OA- 6129D and E, new carbapenam compounds produced by Streptomyces sp. OA-6129, were determined by spectroscopic analysis and chemical transformation.
Anti-Bacterial Agents↗
Structures of OA-6129A, B1, B2 and C, new carbapenem antibiotics produced by Streptomyces sp. OA-6129.
The chemical structures of OA-6129A, B1, B2 and C, new carbapenem antibiotics having a pantetheinyl group at C-3 were elucidated by spectroscopic analysis and chemical transformation as presented in Fig. 1.
Anti-Bacterial Agents↗
Studies on the OA-6129 group of antibiotics, new carbapenem compounds. I. Taxonomy, isolation and physical properties.
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Chemical Phenomena↗
Studies on the OA-6129 group of antibiotics, new carbapenem compounds. II. In vitro evaluation.
The OA-6129 group of antibiotics, new carbapenem compounds, had relatively potent antimicrobial activities against Gram-positive and Gram-negative bacteria. Synergism of compound OA-6129A in combination with conventional beta-lactam antibiotics was observed in antimicrobial activity against beta-lactamase producers such as Proteus vulgaris GN 76 and Citrobacter freundii GN 346. The new carbapenem compounds were slightly superior to PS-5 in stability to kidney homogenates of various animal species.
Animals↗
Pharmacological studies on carbapenem antibiotics. I. Metabolism of PS-5 in animal tissues.
After injection into mice and dogs, PS-5 showed a very rapid decrease in its blood concentration, compared with cefazolin. Using in vitro experiments with tissue homogenates and acetone powder preparations, the kidney was found to be the primary site of PS-5-inactivation, although the extent of the inactivation varied depending on the species of animals. The comparative stability data of PS-5, NS-5 (deacetylated PS-5), thienamycin and N-formimidoylthienamycin in kidney homogenates of mouse, rabbit, dog and man are presented. Bilateral nephrectomy and the injection of ethylenediaminetetraacetate seemed to prolong the survival time of PS-5 in rats and mice respectively.
Animals↗
Pharmacological studies on carbapenem antibiotics. II. Isolation of a PS-5-inactivating factor from the rat kidney.
A factor responsible for the in vivo metabolism of PS-5 was isolated from the microsomal fraction of the rat kidney. This factor, which did not attack penicillins and cephalosporins, was enzymologically identified with particle-bound renal dipeptidase. Under the action of this factor, PS-5 was inactivated to give three products designated PS-5D I, PS-5D II and PS-5D III.
Animals↗
Pharmacological studies on carbapenem antibiotics. III. Chemical structure of PS-5D III, the primary renal metabolite of PS-5.
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Animals↗