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DISCOVERY, FERMENTATION, BIOLOGICAL PROPERTIES AND TAXONOMY OF THE PRODUCING CULTURE
CHAO-MIN LIU, THERON E. HERMANN, BARBARA LA T. PROSSER, NORBERTO J. PA ...
1981 Volume 34 Issue 2 Pages
133-138
Published: 1981
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X-14766A is a novel, chlorine containing polyether antibiotic produced by
Streptomyces inalachitofuscus subsp. downeyi. The antibiotic is active in vitro gainst Gram-positive bacteria and is capable of complexing and transporting monovalent as well as divalent metal cations.
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JOHN W. WESTLEY, RALPH H. EVANS, Jr., LILIAN H. SELLO, NELSON TROUPE, ...
1981 Volume 34 Issue 2 Pages
139-147
Published: 1981
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This report describes the isolation and chemical characterization of antibiotic X-14766A, the first halogen containing polyether antibiotic, from fermented cultures of
Streptomyces malachitofuscus subsp.
downeyi. The structure of this novel antibiotic was determined by X-ray analyses of the thallium and rubidium salts. In addition to the chlorine atom, which is attached to a salicylic acid chromophore, the molecule contains a tricyclic di-spiroketal ring system and an ethyl ester group.
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III. STRUCTURE DETERMINATION OF BBM-928 A, B AND C
MASATAKA KONISHI, HIROAKI OHKUMA, FUMIHIDE SAKAI, TAKASHI TSUNO, HIDEO ...
1981 Volume 34 Issue 2 Pages
148-159
Published: 1981
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Structures of antitumor antibiotics BBM-928 A, B and C have been determined. They are cyclic decadepsipeptides containing 3-hydroxy-6-methoxyquinaldic acid as a chromophore. Two amino acids, not found in nature, L-β-hydroxy-N-methylvaline and
trans-(3
S, 4
S)-4-hydroxy-2, 3, 4, 5-tetrahydropyridazine-3-carboxylic acid, were identified as structural constituents of the antibiotic. In gross structure, BBM-928 resembles the echinomycin group of antibiotics which are cyclic octadepsipeptides having a quinoxaline chromophore, but BBM-928 differs from the latter group by virtue of the lack of a sulfur-containing cross linkage.
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IV. SYNTHESIS OF 2-(2-AMINOTHIAZOL-4-YL)-2-METHOXYIMINOACETIC ACID DERIVATIVES AND RELATED COMPOUNDS
MICHIHIKO OCHIAI, AKIRA MORIMOTO, YOSHIHIRO MATSUSHITA, TAIITI OKADA
1981 Volume 34 Issue 2 Pages
160-170
Published: 1981
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In an effort to improve the antibacterial activity of 7β-[2-(2-aminothiazol-4-yl)acetamido]-cephalosporins by introducing a methoxyimino group into the 7-acyl side chain, geometrically isomeric 2-(2-aminothiazol-4-yl)-2-methoxyiminoacetic acids and their derivatives were selectively synthesized. Structurally related acid derivatives were also synthesized. A facile and practical synthesis of an important starting material, 2-(2-chloroacetamidothiazol-4-yl)-(
Z)-2-methoxyiminoacetic acid, for the preparation of SCE-1365 which is now under extensive clinical trial was achieved.
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V. SYNTHESIS AND ANTIBACTERIAL ACTIVITY OF 7β-[2-(2-AMINOTHIAZOL-4-YL)-2-METHOXYIMINOACETAMIDO]-CEPHALOSPORIN DERIVATIVES AND RELATED COMPOUNDS
MICHIHIKO OCHIAI, AKIRA MORIMOTO, TOSHIO MIYAWAKI, YOSHIHIRO MATSUSHIT ...
1981 Volume 34 Issue 2 Pages
171-185
Published: 1981
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In order to improve the antibacterial activity of 7β-[2-(2-aminothiazol-4-yl)acetamido]-cephalosporins new derivatives having a methoxyimino moiety in the 7-acyl side chain and related compounds were synthesized. Of these, 7β-[2-(2-aminothiazol-4-yl)-(
Z)-2-methoxyiminoacetamido] cephalosporins were found to possess excellent activity against a variety of Gram-positive and Gram-negative bacteria including β-lactamase-producing strains. An extensive study of structure-activity relationships led to the selection of 7β-[2-(2-aminothiazol-4-yl)-(
Z)-2-methoxyiminoacetamido]-3-[(1-methyl-1
H-tetrazol-5-yl)thiomethyl]-ceph-3-em-4-carboxylic acid, SCE-1365, for further biological and clinical evaluation.
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VI. ALTERNATIVE SYNTHESES OF 7β-[2-(2-AMINOTHIAZOL-4-YL)-(Z)-2-METHOXYIMI NO-ACETAMIDO] CEPHALOSPORIN DERIVATIVES
MICHIHIKO OCHIAI, AKIRA MORIMOTO, TOSHIO MIYAWAKI
1981 Volume 34 Issue 2 Pages
186-192
Published: 1981
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Alternative syntheses of 7β-[2-(2-aminothiazol-4-yl)-(
Z)-2-methoxyiminoacetamido]-cephalosporins (
1) were investigated. Of these, a sequence of reactions starting from
6a via 8a, 9a, 13a and
13b afforded a convenient route to 1a which is especially useful for the preparation of labeled cefmenoxime. Structures of nitrone compounds which were formed as by-products are discussed.
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JACK TADANIER, DANIEL A. DUNNIGAN, JERRY R. MARTIN, LESLIE FREIBERG, M ...
1981 Volume 34 Issue 2 Pages
193-201
Published: 1981
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Selective 6'-
N-alkylation of 1, 2'-di-
N-benzyloxycarbonylfortimicin B was effected by both catalytic and chemical reductive alkylation in the presence of aldehydes. These facile selective 6'-
N-alkylations were used as the basis of the preparations of the 6', 6'-di-
N-methylfortimicins A and B, and the 6'-
N-methylfortimicins A and B. Of these new 6'-
N-methylated fortimicins, only 6'-
N-methylfortimicin A has appreciable antibacterial activity, which was about half that of fortimicin A.
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RAJANIKANT J. MEHTA, DAVID J. NEWMANB, BETTY ANNE BOWIE, CLAUDE H. NAS ...
1981 Volume 34 Issue 2 Pages
202-205
Published: 1981
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The stability of cefonicid (SK&F 75073) towards representatives of six major classes of β-lactamases was determined using a spectrophotometric assay. Cefonicid was stable to hydrolysis by the Type I enzyme from
Enterobacter cloacae and by the enzyme from the anaerobe,
Bacteroides fragilis. It was 6 to 7 times more stable than cefamandole to the Type IIIA and B enzymes from
Escherichia coli, a little less stable than this antibiotic to the Type V enzyme from
E. coli, and of equal stability to the Type
IV enzyme from
Klebsiella aerogenes. Cefonicid was a non-competitive inhibitor (Ki of 0.8×10
-6 M) of cephalothin hydrolysis by the Type I enzyme.
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III. MODE OF ACTION
UKIMASA NOZAKI, FUMIKO KAWASHIMA, AKIRA IMADA
1981 Volume 34 Issue 2 Pages
206-211
Published: 1981
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Biochemical activities of new carbapenem antibiotics, C-19393 H
2(H
2) and C-19393 S
2(S
2), were examined in comparison with those of mecillinam using
Escherichia coli. H
2 showed remarkably high affinity for penicillin-binding protein (PBP) 2, and high affinity for PBPs 1 and 3. S
2 showed high affinity for PBP 2, moderate affinity for PBP 1 and low affinity for PBP 3. They induced ovoid cells at lower concentrations and cell lysis at higher concentrations. The inhibitory potency of H
2 for peptidoglycan synthesis was similar to that of mecillinam at lower concentrations up to 0.1μg/ml. At concentrations higher than 0.1 μg/ml, the inhibition rate by H
2 gradually increased up to 100%, whereas that by mecillinam remained at 60% level. The MICs of H
2, S
2 and mecillinam corresponded to the lowest concentrations giving 60% of inhibition of peptidoglycan synthesis at which concentrations the function of PBP 2 seemed to be prevented completely. These findings indicate that the primary targets of H
2 and S
2 are PBP 2 involved in cell shape determination in
E. coli.
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IV. INHIBITORY ACTIVITY AGAINST β-LACTAMASES
KENJI OKONOGI, YUKIMASA NOZAKI, AKIRA IMADA, MITSUZO KUNO
1981 Volume 34 Issue 2 Pages
212-217
Published: 1981
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New carbapenem antibiotics, C-19393 S
2 and H
2, have been found to be potent and broad-spectrum inhibitors of β-lactamases. Among 11 types of β-lactamases tested, those from
Escherichia coli (plasmid-bearing),
Klebsiella pneumoniae,
Proteus vulgaris, Serratia marcescens and
Bacteroides fragilis were especially sensitive. They also inhibited cephalosporinases insensitive to clavulanic acid. The inhibition by C-19393 S
2 and H
2 was of progressive type, except for the inhibition of
E. coli enzyme (plasmid-mediated type I) by C-19393 H
2. The inhibition of
E. coli β-lactamase by C-19393 S
2 was irreversible, while that by C-19393 H
2 was reversible.
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TADATOSHI MIYAGAMI, YOSHIMI TAKEI, YOSHITSUGU MATSUMOTO, NOBORU OTAKE, ...
1981 Volume 34 Issue 2 Pages
218-223
Published: 1981
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Lonomycin A at various concentrations was tested for its inhibitory effect on
Toxoplasma multiplication in host cells cultured
in vitro. Results indicated that lonomycin A at a concentration of 0.01μg per ml in TC-199 medium demonstrated a high degree of antitoxoplasma activity with complete inhibition of
Toxoplasma multiplication in the host cells. Lymphokines, a supernatant produced from spleen cells of mice infected chronically with
Toxoplasma gondii, inhibited
Taxoplasma multiplication in mice macrophage and kidney cell monolayers. However, lonomycin A inhibited completely
Toxoplasma multiplication in non-specific cells,
i.e. not only in mice macrophages and kidney cells but also in cells of human and other animal species.
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MEGUMI KONO, HAJIME HAMASHIMA, KOJI O'HARA
1981 Volume 34 Issue 2 Pages
224-230
Published: 1981
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Clinical isolates of
Streptococcus faecalis were found to contain streptomycin (SM)-phosphotransferase, kanamycin (KM)-acetyltransferase and KM-adenylyltransferase. The existence of a new type of KM-phosphotransferase was suggested from aminoglycoside substrate profiles.
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TAKESHI NISHI, MASAFUMI NAKAO, KANM TSUCHIYA
1981 Volume 34 Issue 2 Pages
231-239
Published: 1981
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The MICs of cefotiam and cefazolin against
K. pneunzoniae DT-S were Unaffected by the inoculum size and were 0.1 and 1.56μg/ml, respectively. Bactericidal and bacteriolytic activities of the cephalosporins were more potent in bacterial concentrations of 10
7 colonyforming units (CFU)/ml than in concentrations of 10
8 CFU/ml. Both activities of cefotiam were more markedly influenced by bacterial concentrations than those of cefazolin. Therapeutic activity of cefotiam was about 9-15 times as potent as that of cefazolin in experimental pneumonia caused by
K. pneumoniae DT-S in mice, and this finding was in accordance with the ratio of
in vitro antibacterial activities of the two cephalosporins as judged by the MICs or the bactericidal and bacteriolytic activities in bacterial suspension of 10
7 CFU/ml. The range of concentrations of cefotiam which induced cell filamentation
in vitro, was wider than that of cefazolin. This difference, however, was not reflected on the therapeutic activities of the two cephalosporins in the model infection. In the pneumonic lungs, definite therapeutic doses of both cephalosporins (80 mg of cefotiam per kg and 640 mg of cefazolin per kg) produced mainly bacteriolysis of the challenge organisms.
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III. NEW DEOXY DERIVATIVES OF PAROMOMYCIN1)
CARLO BATTISTINI, GIUSEPPE CASSINELLI, GIOVANNI FRANCESCHI, FEDERICO A ...
1981 Volume 34 Issue 2 Pages
240-242
Published: 1981
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CHIKAHIRO URAKAWA, HARUKO TSUCHIYA, KIN-ICHI NAKANO
1981 Volume 34 Issue 2 Pages
243-244
Published: 1981
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YASUTAKA SHIMAUCHI, MICHIKO SAKAMOTO, KOSUMI HORI, TOMOYUKI ISHIKURA, ...
1981 Volume 34 Issue 2 Pages
245-248
Published: 1981
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YUKIO SUGIURA, TOMOHISA TAKITA, HAMAO UMEZAWA
1981 Volume 34 Issue 2 Pages
249-251
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ROBERT THOMAS, DAVID J. WILLIAMS
1981 Volume 34 Issue 2 Pages
252-254
Published: 1981
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OSAMU NIMI, ARNOLD L. DEMAIN
1981 Volume 34 Issue 2 Pages
255-257
Published: 1981
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