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Volume 67 (1970)
- Issue 6 Pages 753-
- Issue 5 Pages 611-
- Issue 4 Pages 507-
- Issue 3 Pages 333-
- Issue 2 Pages 157-
- Issue 1 Pages 1-
Volume 67, Issue 4
Displaying 1-14 of 14 articles from this issue
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MICHITERU YOSHIDA, KENSUKE SHIMURA1970 Volume 67 Issue 4 Pages 507-512
Published: April 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSIn order to elucidate the biological function of histories, specific repression of RNA synthesis primed by chromatins from posterior or middle silk gland by histones of these silk glands was studied. The whole histone of one kind of silk gland exerted a slight repression on the RNA synthesis primed by chromatin from the same kind of silk gland, although the whole histone from another kind of silk gland repressed it intensively. Such a specific repression observed in the system with chromatin was not detected ut the system with a reconstituted nucleoprotein from DNA and histone of each silk gland. These results may indicate that histones of two kinds of silk gland comprize some dif-ferent species of histone. A possible mode of specific repression for the RNA synthesis by histones was discussed.View full abstractDownload PDF (771K) -
IX. Chemical Modification of the Enzyme by MonoiodoacetamideMASATO OHE, BYEONG-KUK SEON, KOITI TITANI, YUJI TONOMURA1970 Volume 67 Issue 4 Pages 513-522
Published: April 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe Mg2+- and Ca2+-ATPase activities of myosin [ATP phosphohydrolase; EC 3. 6. 1. 3] were activated 10-15 fold, but the EDTA-ATPase activity was inhibited 80% by carboxamidomethytation of a specific cysteine residue of myosin by IAA****. The pH-activity curve of carboxamidomethyl myosin ATPase was very similar to that of untreated myosin ATPase.
When myosin was treated with IAA in the presence of urea, 2 moles of cysteine residues in the Ile•CySH•Arg sequences per mole of myosin were modified. However, treatment of native myosin with IAA resulted in carboxamidomethylation of 1 mole of cysteine residue of this sequence per mole of myosin, and this modified the ATPase actiyity, as described above.View full abstractDownload PDF (539K) -
XIV. Partial Chemical Structure of One Component of Clupeine, Clupeine ZMASAO AZEGAMII, SHIN-ICHI ISHII, TOSHIO ANDO1970 Volume 67 Issue 4 Pages 523-532
Published: April 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. One homogeneous component (Z) was separated by chromatography on an alumina column from clupeine sulfate which was prepared from sperm heads of Pacific herrings (Clupea pallasii).
2. The amino acid composition of clupeine Z was determined by the analyses of both the acid hydrolyzate and the tryptic peptides, which gave a molecular formula, Ala3•Ser3•Pro2•Val2•Arg21 for clupeine Z. The calculated molecular weight was 4163 as a free base and 4929 as its hydrochloride, while that estimated from the amount of DNP groups introduced into the protamine was approximately 5, 500 as hydrochloride.
3. The amino acid sequence of clupeine Z was studied by using an endopeptidase (trypsin [EC 3. 4. 4. 4]), exopeptidases (leucine aminopeptidase [EC 3. 4. 1. 1] and carboxvpeptidases A [EC 3. 4. 2. 1] and B [EC 3. 4. 2. 2]). A partial structure proposed for clupeine Z was as follows: H-Ala•Argm•Ser•Argn•Ala•Ser•Arg•Pro•Val•Argp•Pro•Argq•Val•Ser•Argr•Ala•Arg4-OH, where m+n=6, p+q+r=10, and q+r≤5.View full abstractDownload PDF (623K) -
TAKIKO AKINO, MINORU AMANO1970 Volume 67 Issue 4 Pages 533-539
Published: April 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe ability of stimulating amino acid incorporation into protein by various nuclear RNA fractions (nucleolus, chromatin and nuclear sap) of the ascites hepatoma, AH-l30 cells was investigated by a protein synthesizing system derived from Escherichia coli. Nuclear sap RNA had the highest template activity; the degree of stimulation of 14C-leucine incorporation into protein by it was 5 times as high as that by chromatin RNA. The template activity of nucleolar RNA was slightly higher than that of chromatin RNA. The distribution of RNA molecular species having the capacity for stimulating 14C-leucine incorporation in nuclear sap and chromatin RNA displayed polydisperse patterns with the maximum activity in the RNA of 18S region. From the comparison of the ability to incorporate leucine, arginine and phenylalanine by three nuclear RNA fractions, the ratio of the incorporated arginine to the incorporated leucine (arginine/leucine) by nucleolar RNA was 1.31 and that by chromatin RNA was 0.97 but that by nuclear sap RNA was 0.48. The ratio of phenylalanine/leucine incorporated by three nuclear RNAs was about 0.6.View full abstractDownload PDF (430K) -
VIII. Reaction of 2-Hydroxy-5-nitrobenzyl Bromide with the Single Tryptophan Residue in Ribonuclease T1KENJI TAKAHASHI1970 Volume 67 Issue 4 Pages 541-547
Published: April 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The reaction of 2-hydroxy-5-nitrobenzyl bromide with ribonuclease T1 [EC 2. 7. 7. 26] has been investigated in order to obtain some information on the role of the single tryptophan residue at position 59 in the function of this enzyme. Ribonuclease Tt (0.08 to 0.29%, solution) was treated with 280- to 1, 000-fold molar excess of the reagent at pH 5.0 or 3.5 and 25°C in the presence and absence of 8nt urea.
2. In the absence of urea, no significant reaction took place and the enzyme retained over 90% of the original activity after treatment at pH 5.0 for 30min. This indicates that the tryptophan residue-59 in the enzyme is buried in the interior of the protein molecule or bound to some other residue or residues, thus becoming unreactive.
3. The reaction took place very rapidly when the reaction was carried out in the presence of 8 a urea at pH 5.0 or 3.5 and the enzymatic activity toward both RNA and 2', 3'-cyclic guanylic acid was lost in parallel. The inactivation almost paralleled the incorporation of one residue per molecule of 2-hydroxy-5-nitrobenzyl group into the indole ring of the tryptophan residue. The final product prepared at pH 3.5 which was almost devoid of activity, however, contained nearly two residues of 2-hydroxy-5-nitrobenzyl group per molecule.
4. The amino acid composition of acid hydrolysates of the inactivated protein was indistinguishable from that of the native protein. This indicates that the reaction took place specifically with the tryptophan residue in the enzyme. The results of analysis of a Nagarse peptide fraction containing 2-hydroxy-5-nitrobenzyl group are in support for this conclusion.
5. The reactivity of the γ-carboxyl group of the adjacent glutamic acid residue at position 58 toward iodoacetate was markedly diminished by the modification of the tryptophan residue with the reagent.
6. These lines of evidence indicate that the tryptophan residue-59 in ribonuclease Tt is probably not directly involved in the catalytic process, but is very likely to be one of the important elements in building up the architecture of the active center of the enzyme.View full abstractDownload PDF (457K) -
I. Sensitivity of the Complexes to Nucleolytic EnzymesMAKOTO KAGEYAMA, MAMORU HASEGAWA, AKIYO INAGASI, FUJIO EGAMI1970 Volume 67 Issue 4 Pages 549-557
Published: April 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe interactions of several antibiotics with deoxyribonucleic acid were studied by the sensitivities of their complexes to nucleolytic enzymes. After treatment with mito-mycin, DNA was hydrolyzed slower than normal DNA with snake venom phospho-diesterase [EC 3. 1. 4. 1] but at the same rate with pancreatic DNase I [EC 3. 1. 4. 5]. Actinomycin D, quinomycin A, triostin C and chromomycin A3 strongly inhibited the digestion of DNA with DNase I, chromomycin being the strongest inhibitor. The interactions of these drugs with DNA were studied by spectrophotometric titration. In general it was found that the sensitivity to DNase decreases by half when the binding sites are just filled by these drugs.View full abstractDownload PDF (466K) -
IV. The Cellular Components Excreted into the Media during Different Deprivation ConditionsHIROMI MARUYAMA, MITSUKO ONO-ONITSUKA, DEN'ICHI MIZUNO1970 Volume 67 Issue 4 Pages 559-565
Published: April 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSTime course studies and analysis of the compounds excreted into the media was carried out during Mg- and P-deprivation, and complete starvation.
The rate of excretion of nucleic acid components was faster during complete starvation than during Mg-deprivation; while no release of phosphate and very little release of UV-absorbing material and ribose were seen during P-starvation. The characteristic release of protein (Folin positive substances) and sugar (anthrone positive substances) were found in every case. Analysis of the released materials after Sephadex G-25 column chromatography showed that large protein and sugar molecules were released in considerable amounts during each of the starvation conditions studied.View full abstractDownload PDF (419K) -
HIROBUMI TERAOKA, TSUKASA NISHIKIDO, KATSURA IZUI, HIROHIKO KATSUKI1970 Volume 67 Issue 4 Pages 567-575
Published: April 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The level of phosphoenolpyruvate (PEP) carboxylase [EC 4. 1. 1. 31] in Escherichia coli W was remarkably affected by the carbon source in the growth medium. The enzyme level was found to decrease in the following order: glucose>glycerol>malate> lactate>acetate>aspartate. Several lines of evidence support that PEP carboxylase is nutritionally induced by glucose but not repressed by any compound related to the tricarboxylic acid cycle.
2. The level of PEP carboxykinase [EC 4. 1. 1. 49] in the cells grown on malate-, aspartate-, or enriched media was 4- to 7-fold higher than that on glucose media. The synthesis of PEP carboxykinase was presumed to be nutritionally repressed by glucose.
3. In view of the antagonistic behaviors of these two enzymes in the cells grown on various carbon sources, the syntheses of both enzymes seem to be inversely regulated each other. The regulatory mechanism concerned in the syntheses of these two physio-logically antagonistic enzymes was supposed to play an important role in the metabolic shift from glycolysis to gluconeogenesis, or vice versa.View full abstractDownload PDF (563K) -
I. Effect of Starvation on Ribonucleic Acid Degradating and Synthesizing SystemsTOSHIO ONISHI1970 Volume 67 Issue 4 Pages 577-585
Published: April 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSRats were fasted for different periods (1-9 days) and their body weight decreased by 10 to 45% of the initial weight. During starvation, the contents of nuclear RNA-P, ribosomal RNA-P and soluble RNA-P, expressed in μg P per μg DNP-P of the liver, decreased exponentially with loss of body weight and at approximately the same relative rates.
During starvation the polysome profile alters and the polysome content decreases.
On loss of up to 20-25% body weight, the activities of both the free and latent forms of alkaline RNase (units/μg DNA-P) are maintained. However, they decrease to 50% of the normal level on loss of 40-45% body weight. Acid RNase activity and activity of alkaline RNase inhibitor decrease with loss of body weight.
The activity of DNA-dependent RNA polymerase [EC 2. 7. 7. 6], prepared as an aggregate-enzyme, decreases nearly in parallel with decrease in levels of various RNA's during starvation.
Starvation also results in decrease in the levels of ribonucleotides in liver cells.View full abstractDownload PDF (575K) -
NOBORU YAMAMOTO, HIDEO HATAKEYAMA, KATSUZO NISHIKAWA, TAKEKAZU HORIO1970 Volume 67 Issue 4 Pages 587-598
Published: April 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe quinones associated with chromatophores from Rhodospirillum rubrum are ubiquinone-10 (UQ 10) and rhodoquinone. The effects of extraction of the quinones and addition of several quinones on various activities have been studied.
When the quinones are extracted, the activity in the light for ATP formation, the activities in darkness for ATP hydrolysis and ATP-Pi exchange, and the activities in darkness for reduction of cytochrome c2 by NADH and oxidation of NADH by O2, are depressed. These depressed activities are restored to the original level when extracted chromatophores are supplemented with UQ-l0. The other ubiquinones tested are equally effective in restoring the activities. Rhodoquinone, plastoquinone, α-tocopherolquinone and phylloquinone are as effective as UQ-10 in restoring the activities for ATP hydro-lysis and ATP-Pi exchange, whereas they are significantly less effective than UQ-10 in restoring the other activities. With chromatophores reconstructed by addition of UQ-10, the effect of oligomycin, antimycin A and redox-reagents is also reported.
In “intact” chromatophores, the activities for ATP formation, ATP hydrolysis, ATP-Pi exchange and electron transport are in a major part exhibited by the enzyme systems containing UQ-10. Probably, UQ-10 is the factor coupling between the electron transport system and the energy conservation system leading to ATP formation, serving as the primary step for energy conservation.View full abstractDownload PDF (687K) -
KUNIO YAGI, NOBUKO OHISHI1970 Volume 67 Issue 4 Pages 599-601
Published: April 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (202K) -
I. Cytochrome b-563 from Larvae of the Housefly, Musca domestica LYOSHIIE OKADA, KAZUO OKUNUKI1970 Volume 67 Issue 4 Pages 603-605
Published: April 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (208K) -
MASAMI GAMO, KUNIHIKO SAITO1970 Volume 67 Issue 4 Pages 607-608
Published: April 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (1265K) -
KOUI TAKAHASHI, AKIHITO HATTORI, TSUTOMU YASUI1970 Volume 67 Issue 4 Pages 609-610
Published: April 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (124K)
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