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THE RECOMBINATION OF MITOCHONDRIAL DRUG RESISTANCES
KAZUHIKO WAKABAYASHI
1974 Volume 27 Issue 6 Pages
373-378
Published: 1974
Released on J-STAGE: April 12, 2006
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Mutants of yeast with mitochondrial chloralnphenicol-resistance, erythromycin-resistanceand oligomycin-resistance were crossed and the recombination values werestudied. Crosses were compared, which were performed between the cells of the same type and of different types (type I and type II). The recombination values between erythromycin-resistance and oligomycin-resistance did not show any significant change in both crosses, but increased rates of recombination between chloramphenicol-resistance and other two resistance markers were found in the latter crosses. It was also observed in these crosses that the recombination values for [cap]-[oli] was close to the addition of the values for [cap]-[ery] and for [ery]-[oli].
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JEFFREY L. SCHWARTZ, MICHIKO KATAGIRI, SATOSHI OMURA, MAX TISHLER
1974 Volume 27 Issue 6 Pages
379-385
Published: 1974
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Examination of the effects of prumycin on sensitive
Botrytis cinerea and
Sarcinalutea showed that inhibition of protein synthesis in both organisms and reduction in ribonucleic acid synthesis in
Botrytis cinerea are among the mechanisms of action. The inhibition of RNA biosynthesis in
Botrytis cinerea is probably a secondary effect Resulting from the termination of protein synthesis rather than a direct inhibition. In a cell-free protein-synthesizing system obtained from crushed
Botrytis cinerea cells, incorporation of L-phenylalanine-
14C into polyphenylalanine (with polyuridylic acid as synthetic messenger) was inhibited by prumycin. Ribosome binding studies indicated that prumycin did not effect its inhibition at the ribosomal stage of protein synthesis.
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I. PRODUCING ORGANISM, FERMENTATION AND ISOLATION, BIOLOGICAL ACTIVITIES AND PHYSICAL AND CHEMICAL PROPERTIES
TATSUO HANEISHI, NOBUAKI KITAHARA, YOO TAKIGUCHI, MAMORU ARAI, SHINICH ...
1974 Volume 27 Issue 6 Pages
386-392
Published: 1974
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Methylenomycins A and B, two new antibiotics were found in the culture filtrate of a streptomycete strain No.2416, which was identified as a strain of
Streptomyces violaceoruber. Their elementary analyses and mass spectroscopic measurements suggested that the molecular formula of methylenomycin A was C
9H
10O
4 and that of methylenomycin B was C
8H
10O
2. Methylenomycins A and B exhibited activities against gram-positive and gram-negative bacteria, and especially against
Proteus.
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II. STRUCTURES OF METHYLENOMYCINS A AND B
TATSUO HANEISHI, AKIRA TERAHARA, MAMORU ARAI, TADASHI HATA, CHIHIRO TA ...
1974 Volume 27 Issue 6 Pages
393-399
Published: 1974
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The structure of methylenomycin A was studied physico-chemically and finally established by X-ray crystallographic analysis as 2-methylene-cyclopentane-3-one-4, 5-epoxy4, 5-dimethyl-1-carboxylic acid. The structure of methylenomycin B was also determined by a comparative study of the nuclear magnetic resonance spectra of methylenomycins A and B to be 4, 5-epoxy4, 5-dimethyl-2-methylene-cyclopentane-3-one, which makes it a decarboxylated derivative of methylenomycin A.
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III. CHEMICAL MODIFICATIONS OF METHYLENOMYCIN A AND STRUCTURE-ACTIVITY CORRELATIONS IN METHYLENOMYCINS
TATSUO HANEISHI, AKIRA TERAHARA, KIYOSHI HAMANO, MAMORU ARAI
1974 Volume 27 Issue 6 Pages
400-407
Published: 1974
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Chemical modification of methylenomycin A afforded broadened spectrum as well as stronger antibiotic activity. In addition to the original antibacterial activity of methylenomycin A, the alkyl ester derivatives of the antibiotic possessed antifungal activity. With regard to structure-activity relationship, the existence of theα, β-unsaturated carbonyl function, epoxide and cyclopentane ring was found to be essential for antibacterial activity, and the alkyl ester, C
3-carbonyl group, epoxide and cyclopentane ring for the antifungal activity.
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K. HORÀKOVÀ, J. NAVAROVÀ, P. NEMEC, M. KETTNER
1974 Volume 27 Issue 6 Pages
408-412
Published: 1974
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Dactylarin is a new antiprotozoal antibiotic which also exhibits cytotoxic activity. The decrease of mitotic index in treated HeLa cells indicates that the antibiotic inhibition is expressed prior to mitosis. Dactyiarin inhibited the progression or G
2 cells into mitosis. One of the earliest changes of dactylarin-treated cells was an increase in the cell size. Dactylarin induced unbalanced growth of HeLa cells in which DNA and RNA content per unit of cell volume decreased. while protein content remained directly proportional to the increased cell volume, Under the same experimental conditions only a slight effect on glucose utilization was observed. In the light of these findings, the possible lethal action of dactylarin was discussed.
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SETSUKO KUNIMOTO, TAKAAKI AOYAGI, RINZO NISHIZAWA, TOMOYOSHI KOMAI, TO ...
1974 Volume 27 Issue 6 Pages
413-418
Published: 1974
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Pepstatin, a strongly bound inhibitor of acid proteases, does not instantaneously bind to pepsin. The dissociation constant of pepsin-pepstatin complex is 9.7 × 10
-11 M using Phe•Gly•His•Phe(NO
2)•Phe•Ala•PheOMe as substrate. Difference ultraviolet absorption spectra show conformational change of pepsin in interaction with pepstatin. The bindillg of pepsin with pepstatin is stoicheometric and the normality of pepsin can be easily titrated by pepstain. Pepsin modified by 1, 2-epoxy-3-(p-nitrophenoxy) propane, 2, 3-butanedione, α-diazo-p-bromoacetophenone or p-bromophenacyl bromide shows reduced pepstatin-binding activity.
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HAMAO UMEZAWA, SENJI HORI, TSUTOMU SAWA, TAKEO YOSHIOKA, TOMIO TAKEUCH ...
1974 Volume 27 Issue 6 Pages
419-424
Published: 1974
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Affinity chromatography of a bleomycin-inactivating enzyme was studied on Sepharose 4 B-bleomycin A
5 and Sepharose 4 B-lysinamide. Mouse liver was homogenized, and the enzyme extracted by ammonium sulfate precipitation and Sephadex G-200 chromatography. Affinity chromatography of the extract on Sepharose 4 B-lysinamide gave 25-fold purified enzyme, Further purification vas not successful because of instability of the enzyme. It hydrolyzed L-lysinamide, L-lysyl-β-naphthyl-amide, L-arginy1-β-naphthylamide, L-lysyl-L-lysine and Iysyl-bradykinin, but not leucinamide or L-leucyl-β-naphthylamide. Hydrolysis of L-lysyl-β-naphthylamide and L-arginyl-β-naphthylamide by the enzyme was competitively inhibited by bleomycin B
2. The bleomycin-inactivating enzyme of rat liver was separated from a known aminopeptidase B.
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DEACYLATION OF MARIDOMYCIN BY BACTERIA
KAZUO NAKAHAMA, MOTOWO IZAWA, MASAYUKI MUROI, TOYOKAZU KISHI, MINORU U ...
1974 Volume 27 Issue 6 Pages
425-432
Published: 1974
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Maridomycin, a macrolide antibiotic, was hydrolyzed to 4"-deacylmaridomycin byesterases obtained from many bacteria. Among these bacteria, Bacillus megaterium91277 showed the highest activity. The properties of the esterase were investigated by using cell-free extract obtained from B.
megaterium 91277. Optimum pH was 8.5.9-Propionylmaridomycin was also hydrolyzed to 4"-deacyl-9-propionylmaridomycin by the esterase. The hydrolytic rate of 9-propionylmaridomycin was more rapid than that of maridomycin. Substrates bearing 4"-acyl group of C
3 or C
4 were most rapidly hydrolyzed. 4"-Depropionylmaridomycln III and 4"-depropionyl-9-propionylmaridomycin III were prepared from maridomycin III and 9-propionylmaridomycin III, respectively, in large scale by using culture broth of B.
megaterium 91277. 4"-DeisovaIeryljosamycin
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HYDROXYLATION OF MARIDOMYCIN I AND JOSAMYCIN
KAZUO NAKAHAMA, TOYOKAZU KISHI, SEIZI IGARASI
1974 Volume 27 Issue 6 Pages
433-441
Published: 1974
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Maridomycin I (MDM I), a macrolide antibiotic, was hydroxylated at β-position of 4"-isovaleryl group to 3'''-hydroxymaridomycin I (HMDM I) by culture broth of
Streptomyces olivaceus 219. The structure of HMDM I was elucidated from the results of its NMR and mass spectra, methanolysis and alkaline hydrolysis. Josamycin (JM) was also hydroxylated to 3'''-hydroxyjosamycin (HJM) by the same strain. Antimicrobial activities of these hydroxylated products (HMDM I and HJM) were 1/2-1/5 of their substrates(MDM I and JM), Protective effect of HJM against
Staphylococcus aureus by oral administration, however, was similar to that of JM. HJM and HMDM I were resistant to rat liver homogenate and bacterial esterase, which hydrolyzed JM and MDM I to 4"-deisovaleryljosamycin and 4"-deisovalerylmaridomycin I, respectively.
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INCORPORATION OF LABELED PRECURSORS INTO MARIDOMYCIN AND PREPARATION OF 14C-LABELED 9-PROPIONYLMARIDOMYCIN
HIDEO ONO, SETSUO HARADA, TOYOKAZU KISHI
1974 Volume 27 Issue 6 Pages
442-448
Published: 1974
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investigated by using
Streptomyces hygroscopicus. Of some compounds, L-methionine-methyl-
14C was well incorporated into maridomycin molecule with 27% of the added radioactivity. Degradation studies of the labeled maridomycin revealed that one methyl group in aglycone, two methyl groups in mycaminose and one methyl group in mycarose were derived from the methyl group of L-methionine.
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ISOLATION AND STRUCTURES OF METABOLITES OF 9-PROPIONYLMARIDOMYCIN
MASAYUKI MUROI, MOTOWO IZAWA, TOYOKAZU KISHI
1974 Volume 27 Issue 6 Pages
449-459
Published: 1974
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9-Propionylmaridomycin (PMDM) and maridomycin (MDM) were transformed into 4"-deacyl-9-propionylmaridomycin (PMDM-M) and 4"-deacylmaridomycin (MDM-M), respectively, by incubation with rat liver homogenates in pH 7.2 buffer solution. The structures of these products were elucidated from their physicochemical properties and the result of chemical conversions into the known derivatives of MDM. Furthermore, PMDM-M was isolated as a main metabolite from the urine of rats treated with PMDM by oral route. On the other hand, from human urine after oral administration of PMDM, three metabolites were recovered and identified as PMDM-M, MDM and MDM-M by direct comparison.
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THE 4'-DEOXYBUTIROSINS (BU-1975C1 AND C2), NEW AMINOGLYCOSIDE ANTIBIOTICS OF BACTERIAL ORIGIN
HIROSHI KAWAGUCHI, KOJI TOMITA, TOSHIO HOSHIYA, TAKEO MIYAKI, KEI-ICHI ...
1974 Volume 27 Issue 6 Pages
460-470
Published: 1974
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Strains of
Bacillus circulans produced the new aminoglycoside antibiotics, 4'-Deoxybutirosins A and B (Bu-1975C
1 and C
2). The new antibiotics C
21H41N5O11, have physicochemical properties similar to butirosins A and B (C21H41N5O12) with specific differences in TLC and NMR. The antibacterial activity and spectra of 4'-deoxybutirosins are similar to but broader than that of butirosins, inhibiting some butirosin-resistant organisms and showing increased anti-pseudomonal activity. The acute intraveous toxicity of Bu-1975C1 is lower than that of kanamycin and similar to butirosin A.
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STRUCTURE DETERMINATION OF 4'-DEOXYBUTIROSINS (BU-1975C1 and C2)
MASATAKA KONISHI, KEI-ICHI NUMATA, KUMIKO SHIMODA, HIROSHI TSUKIURA, H ...
1974 Volume 27 Issue 6 Pages
471-483
Published: 1974
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The structures of Bu-1975C
1 and C
2 have been determined to be 4'-deoxybutirosins A and B. They contain the new deoxyaminosugar, 2, 6-diamino-2, 4, 6-trideoxy-α-D-xylo-hexopyranose (4-deoxyneosamine C).
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NOBORU OTAKE, KAZUO FURIHATA, KATSUMI KAKINUMA, HIROSHI YONEHARA
1974 Volume 27 Issue 6 Pages
484-486
Published: 1974
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DEACYLATION OF MARIDOMYCIN BY ACTINOMYCETES
KAZUO NAKAHAMA, TOYOKAZU KISHI, SEIZI IGARASI
1974 Volume 27 Issue 6 Pages
487-488
Published: 1974
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SENJI HORI, TSUTOMU SAWA, TAKEO YOSHIOKA, TOMOHISA TAKITA, TOMIO TAKEU ...
1974 Volume 27 Issue 6 Pages
489-491
Published: 1974
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