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Volume 59, Issue 1
Displaying 1-17 of 17 articles from this issue
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I. Isolation, Purification and Some Properties of Cytochrome b from Beef Heart MuscleKEN OHNISHI1966 Volume 59 Issue 1 Pages 1-8
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A highly purified preparation of cyto-chrome b was obtained from beef heart muscle by cholate-extraction, isolation by precipitation, solubilization with proteinase, ammonium sulfate fractionation, gel filtration, and chromatography on DEAE-cellulose.
2. The absorption spectra of the purified cytochrome b were observed and the extinc-tion ratios of the maxima were calculated.
3. The heme content of the preparation was determined to be 47.0 μmoles/g. protein, and the minimum molecular weight was calculated to be 21, 300. The molar extinction coefficients were also calculated.
4. The reduced cytochrome b was auto-xidizable and could combine with carbon monoxide. Under anaerobic conditions, the purified cytochrome b was reduced by lactate in the presence of yeast L-lactate dehydro-genase and this reaction was markedly ac-celerated by the addition of a catalytic amount of redox-dye as a mediator.
5. The heme group of the purified cytochrome b was identified as protoheme.
The author wishes to thank Prof. K. Okunuki for his kind advice and Drs. I. Sekuzu and Y. Orii for their helpful discussion and suggestions during this work.View full abstractDownload PDF (598K) -
II. Crystallization and Some Properties of Cytochrome b from Larvae of the Housefly, Musca domestica LKEN OHNISHI1966 Volume 59 Issue 1 Pages 9-16
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A crystalline cytochrome b was obtained from larvae of the housefly by ammonium sulfate fractionation, treatment with three kinds of ion exchange resin and chromato-graphy on a hydroxylapatite column.
2. The absorption spectra of the crystal-line sample showed maxima at 563, 530 and 428.5mμ in the reduced form and at 520-570 and 418.5 mμ in the oxidized form.
3. The pyridine ferrohemochrome was prepared from purified cytochrome b and the heme content was calculated to be 46.2 μmoles/g. protein. The molar extinction coefficients were calculated to be 28.2×103 and 17.4×l03M-1cm.-1 for the absolute and difference absorbancies at 563mμ, respectively.
4. The molecular weight of the crystal-line sample was determined to be 23, 000 by the sedimentation equilibrium method.
5. The purified cytochrome b was slightly autoxidizable and did not combine with carbon monoxide.
6. Larval cytochrome b could be reduced with yeast lactate dehydrogenase in the pre-sence of sodium lactate and methylene blue under aerobic conditions. However, the reduction of this cytochrome by NADH, suc-cinate, or α-glycerophosphate in the presence of a larval particulate preparation, was un-successful.
7. Peroxidase activity could not be detected in the crystalline sample.
The author is greatly indebted to Prof. K. Okunuki and Drs. I. Sekuzu, H. Matsubara and Y. Orii for their kind advice during this work.View full abstractDownload PDF (1190K) -
III. Comparison of Cytochrome b's from Beef Heart Muscle and Larvae of the HouseflyKEN OHNISHI1966 Volume 59 Issue 1 Pages 17-23
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The GO-affinity of the cytochrome b's from housefly larvae and beef heart muscle were discussed.
2. Preliminary analyses of the amino acid compositions of the two cytochrome b's were made. The molecular weight obtained by these analyses were in good agreement with those obtained by other methods. The contents of hydrophobic residues in the two cytochromes were compared.
3. By ultracentrifugal studies, it was found that the beef heart cytochrome b pre-paration was made up of aggregates, whereas the purified preparation of larval cytochrome b was monomeric.
4. Beef heart cytochrome b could be reduced with NADH in the presence of yeast NADH-cytochrome c reductase but larval cyto-chrome b had no affinity for this enzyme system.
5. The. oxidation-reduction potentials of the two cytochromes were determined. The E0' value of beef heart cytochrome b was lower than that of larval cytochrome b.
The author wishes to thank Prof. K. Okunuki for his valuable advice during this work and Dr. H. Matsubara and Dr. Y. Orii for their technical guidance in amino acid and ultracentrifugal analyses.View full abstractDownload PDF (2159K) -
I. Specific Blocking of the SH Group Responsible for the Inhibitory Phase in “Blphasic Response” of the Catalytic ActivityMASAHIRO YAMAGUCHI, TAKAMITSU SEKINE1966 Volume 59 Issue 1 Pages 24-33
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The S1-blocked myosin obtained by adding 4 equivalents of NEM to myosin subunit, was submitted to the second modifi-cation with 2 equivalents of NEM in the presence of its substrates.
2. The elevated Ca2+-ATPase activity of S1-blocked myosin did not change on adding NEM alone, but was markedly inhibited in the presence of its substrates. The order of magunitude of the effect was ADP>ATP>ITP, PP1+Mg2+>GTP. AMP or PP1 alone was not effective at all.
3. The effect of ATP showed a sharp pH dependence, completely disappearing below pH 6.7. The effect did not change in the varied concentration of KCI from 0.1 to 0.5M.
4. The effect of ADP increased linearly with increase of its concentration expressed on the logarithmic scale, while that of ATP was saturated at the equimolar point with regards to the ratio of ATP to myosin subunit.
5. It was concluded from the determina-tion of the SH content of modified myosins that the number of the specific sulfhydryl group responsible for the Ca2+-ATPase of Sl-blocked myosin is one per subunit. The conformational change around the active site of myosin ATPase induced by its substrates was discussed on the basis of the results obtained.View full abstractDownload PDF (1656K) -
II. Crystallization of the Serine Dehydratase Inhibitor-Forming Enzyme and Its Identity with Cystathionase, Homoserine Dehydratase, Cystine Desulfurase and Cysteine DesulfhydraseAKIRA KATO, MASAJI OGURA, HIROSHI KIMURA, TOYOKO KAWAI, MASAMI SUDA1966 Volume 59 Issue 1 Pages 34-39
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The enzyme producing the inhibitor of serine dehydratase [EC 4. 2. 1. 13] from L-cystine was crystallized from rat liver.
2. The serine dehydratase inhibitor-forming activity was proved to be on the same enzyme protein as the activities of homoserine dehydratase [EC 4. 2. 1. 15], cysta-thionase, cystine desulfurase and cysteine desulf hydrase [EC 4. 4. 1. 1].
3. The Km values of the enzyme for L-homoserine, L-cystathionine, L-cysteine and L-cystine were measured.View full abstractDownload PDF (1849K) -
III. Noncompetitive Inhibition of Cystathionine Synthetase-Serine Dehydratase by Elemental Sulfur and Competitive Inhibition of Cystathionase-Homoserine Dehydratase by L-Cysteine and L-CystineAKIRA KATO, MASAJI OGURA, MASAMI SUDA1966 Volume 59 Issue 1 Pages 40-48
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Serine dehydratase [EC 4. 2. 1. 13] was purified 250 fold from livers of rats fed on a high protein diet.
2. Serine dehydratase activity was strongly and noncompetitively inhibited by elemental sulfur, one of the end products of the decom-position of L-cystine by cystine desulfurase.
3. Homoserine dehydratase and cysta-thionase were competitively inhibited by L-cysteine and L-cystine.
4. Regulatory mechanisms in the rat liver enzyme system converting L-methionine to L-cystine are discussed.
The authors gratefully acknowledge the excellent technical assistance given by Miss Toyoko Kawai.View full abstractDownload PDF (623K) -
I. Inhibition of Nucleic Acid Metabolism in Bacillus subtilis CellsMIKIO KAMIYAMA, YOSHITO KAZIRO1966 Volume 59 Issue 1 Pages 49-56
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Chromomycin A3, an antibiotic and antitumor substance produced by Streptomyces griseus No. 7, inhibits the growth of B. subtilis cells while it permits the normal growth of E. coli cells.
2. The incorporation of inorganic P32 or C14-adenine into DNA or RNA by B. subtilis cells was extensively inhibited by the antibiotic. The inhibition of the uptake of S35-sulfate into protein fraction occurred much slower and might probably be due to the secondary effect resulting from the reduced RNA synthesis.
3. The chromatography of the nucleic acids on methylated albumin-kieselguhr column indicated that the inhibitory effect of the antibiotic is not confined to the particular species of cellular RNA's.
The authors would like to express their deep appreciation to Prof. N. Shimazono for his encourage-ment and valuable adviees.View full abstractDownload PDF (526K) -
MOTOAKI ANAI, TOKUJI IKENAKA, YOSHIO MATSUSHIMA1966 Volume 59 Issue 1 Pages 57-62
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A method was described for the pre-paration of a glycopeptide from taka-amylase A which involves the proteolytic digestion by pronase P combined with ion exchange resin and Sephadex column chromatography.
2. The constituents of the glycopeptide were found to be aspartic acid, serine, N-acetylglucosamine, ammonia, mannose, galac-tose and xylose in the molar ratio of 1:1:2:1:6:0.8:0.5.
3. The results of dinitrophenylation, hydrazinolysis and periodate oxidation of the glycopeptide lead to the conclusion that the carbohydrate prosthetic group is linked at the reducing group of one of the glucosamine molecules to β-carboxyl group of aspartic acid via amide nitrogen, and the structure of the glycopeptide is Ser-Asp-NH-carbohydrate.
The authors wish to express their gratitude to Sankyo Co., Ltd., for their kind supply of “Taka-diastase Sankyo” and also to Dr. K. Sugae of Nara Women's University for performing amino acid analyses.View full abstractDownload PDF (474K) -
IV. The Chemical Structure of UDP-X3AKIRA KOBATA1966 Volume 59 Issue 1 Pages 63-66
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA trisaccharide containing uridine nucleo-tide isolated from human milk and colostrum was further studied by periodate oxidation reaction and its chemical structure was pro-posed to be uridine 5'-[0-α-L-fucopyranosyl (1→2) 0-β-D-galactopyranosyl (1→s4) N-acetyl-D-glucosamine-l-dihydrogen-pyrophosphate].
The author expresses his gratitude to Dr. S. Ta-tsuoka, General Manager, and to Dr. K. Kanazawa, Director of the laboratories for permission for the publication of the experimental results. The author also expresses his gratitude to Dr. A. Misaki for his valuable advices and discussion.View full abstractDownload PDF (1077K) -
HIROSHI NAKAZATO, TOKUTARO HISHIZAWA, HIROSHI TERAYAMA1966 Volume 59 Issue 1 Pages 67-71
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Amino acid incorporation of rat liver slices in the presence of actinomycin D at concentration of 0.1μg/ml. was not different from a control, but it showed a decreasing tendency with time during the incubation at the concentration of 1μg actinomycin D/ml., though with a much slower rate compared with the experimental cases where actinomycin D was administered in vivo.
2. Amino acid incorporating activity of liver slices prepared from rats injected intra-peritoneally with actinomycin D showed a remarkable decrease in the activity during the first 2.5 hours after the injection, and then remained for many hours at an almost constant level depending upon the dosage.
3. A half life span of messenger RNA in liver of rats administered with actinomycin D was speculated to be about 1 hour from the above results.View full abstractDownload PDF (419K) -
MEI SATAKE, SACHIKO ABE1966 Volume 59 Issue 1 Pages 72-75
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Nerve cell perikaryon was isolated from rat cereberal cortex in bulk.
2. The size of the nerve cell perikaryon was small and contained 126μμg. of protein, 14μμg. of RNA and 6μμg. of DNA per cell.
3. Intraperitoneally administered labelled amino acids was incorporated into the protein of nerve cell perikaryon and the rate of incor-poration was higher than that of the protein of total cerebral cortex.
The authors are indebted to Prof. H, Koikegami for his advice in microscopical examination and to Prof. K. Ogata for his helpful discussions. This work was supported in part by a grant for Scientific Researches of the Ministry of Education.View full abstractDownload PDF (1432K) -
YUICHI SHIOBARA1966 Volume 59 Issue 1 Pages 76-77
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
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SHIGERU TAKANASHI, KATSUHIRO IHDA, MINORU KAWADA1966 Volume 59 Issue 1 Pages 78-80
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (198K) -
TADASHI SHIMOJO, TADAO ORII, HIROSHI YAMAGUCHI, KIMIYOSHI OHNO1966 Volume 59 Issue 1 Pages 81-83
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
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HITOSHI SHICHI, DAVID P. HACKETT1966 Volume 59 Issue 1 Pages 84-88
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
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MASAKAZU ASAHI, KEI TSUZURAHARA, SHOICHI NAKAJIMA, YUICHI YAMAMURA1966 Volume 59 Issue 1 Pages 89-90
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (98K) -
KUNIO YAGI, MAKOTO NAOI, AKIRA KOTAKI1966 Volume 59 Issue 1 Pages 91-93
Published: January 25, 1966
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (179K)
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