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Volume 71 (1972)
- Issue 6 Pages 931-
- Issue 5 Pages 759-
- Issue 4 Pages 579-
- Issue 3 Pages 371-
- Issue 2 Pages 173-
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Volume 71, Issue 6
Displaying 1-24 of 24 articles from this issue
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I. Occurrence and Nature of an Electron Transfer System in Propionibacterium arabinosumNobuhito SONE1972 Volume 71 Issue 6 Pages 931-940
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe redox enzymes in Propionibacteriunz arabinosum were examined. Succinate de-hydrogenase was found mainly in the particulate fraction (membrane fragments), whereas NADH, α-glycerophosphate and D-lactate dehydrogenases [EC 1. 6. 99. 3, 1. 1. 99. 5 and 1. 1. 2. 4] were distributed in both the particulate and soluble fractions. Comparison of the Km, values and pH optima indicated that both cellular fractions contained the same species of α-glycerophosphate and lactate dehydrogenases. The particulate fraction also contained a b-type cytochrome, flavoproteins, non-heme iron, and phospholipidis. These components, together with the membrane-bound de-hydrogenases, constituted a particular type of electron transfer system which oxidized NADH, α-glycerophosphate and lactate actively. The oxygen uptake with these substrates was considerably inhibited by the addition of fumarate. The nature of the terminal oxidase functioning in the membrane fragments remained to be solved. Based on these observations, a scheme was presented for the electron-transfer system in the membrane fragments of P. arabinosum. This system is similar to the NADH-cytochrome b and succinate-cytochrome b segments of mam-malian mitochondria. It is postulated that succinate dehydrogenases in this system acts as fumarate reductase and is responsible for the reduction step of propionic acid fermentation.View full abstractDownload PDF (851K) -
I. Purification and Properties of RibonucleaseIkuo SUHARA, Fumiko KAWASHIMA-KUSABA, Yoshio NAKAO, Masahiko YONEDA, E ...1972 Volume 71 Issue 6 Pages 941-950
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The nucleases from Acrocylindrium sp. were partially purified and separated into ribonuclease, endonuclease, exonuclease, and phosphodiesterase [EC 3. 1. 4. 1] by means of acetone precipitation, Sephadex G-100 gel filtration, and DEAE-Sephadex A-50 column chromatography.
2. The ribonuclease was further purified by means of Sephadex G-100 gel filtration, DEAE-Sephadex A-50, and hydroxylapatite column chromatography. The ribonu-clease was chromatographically homogeneous and free from other nucleases and phosphomonoesterases [EC 3. 1. 3. 1 or 3. 1. 3. 2].
3. The pH optimum for the ribonuclease activity was about 7.9. 4.
The ribonuclease was stable against heat treatment (100°C, 5min, at pH 7.5).
5. The molecular weight of the ribonuclease was estimated to be about 9, 000 by gel filtration.
6. The enzyme is a guanyloribonuclease [EC 2. 7. 7. 26].View full abstractDownload PDF (770K) -
VI. Effects of Isoleucine and Valine on Threonine Dehydratase Activity and Its FormationRyuichi MIYAJIMA, Isamu SHIIO1972 Volume 71 Issue 6 Pages 951-960
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThreonine dehydratase [L-threonine hydro-lyase (deaminating), EC 4. 2. 1. 16] was purified about 100-fold from sonic extracts of Brevibacterium flavum and properties of the enzyme were examined. The relationship between the activity and the con-centrations of the enzyme did not show linearity. Thus, the specific activity decreased as the enzyme concentration was reduced. However, the relationship be-tween the activity and the incubation time at a fixed enzyme concentration was linear. The enzyme reaction was specific to L-threonine, and neither D-threonine nor L-serine replaced it for the reaction. Pyridoxal phosphate (PAL-P)** activated the enzyme about twice. The optimum pH of the reaction was 8.0 with Tris-HCl buffer. Potassium phosphate activated the enzyme significantly and shifted the optimum pH to 9. The saturation curve of the substrate, L-threonine, was sigmoidal and the Hill coefficient was calculated to be 3.1, indicating that this enzyme is al-losteric, having at least two threonine binding sites. The enzyme activity was specifically inhibited by the end product, L-isoleucine, and was markedly activated by L-valine. In the presence of 10mM threonine, isoleucine concentration giving 50% inhibition was 0.34mM, while 5mM valine activated the enzyme about 30 times. In the presence of valine, the substrate saturation curve became hyperbolic. Vm was not altered by the presence of these effectors. The relationship between iso-leucine and valine was competitive. The inhibition by isoleucine was not so affected by pH of the medium, while the rate of activation by valine markedly depended on the pH, showing about 30-fold activation at pH 7.5 and 13-fold at pH 9.0, with potassium phosphate buffer. Isoleucine strongly protected the enzyme against heat inactivation. However, valine did not show any protective effect. From the gel filtration experiments, the molecular weight was estimated to be about 2×10, which was not affected in the presence or absence of isoleueine or valine.View full abstractDownload PDF (794K) -
Katsuya SHIGESADA1972 Volume 71 Issue 6 Pages 961-972
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSIn Rhodospirillum rubrum it was shown that δ-aminolevulinate was actively meta-bolized through a new pathway in addition to the pathway for tetrapyrrole biosyn-thesis. The major metabolic products produced through the new pathway from [4-14C] ô-aminolevulinate were ô-amino-γ-hydroxyvalerate, α-hydroxyglutarate and glutamate. Based on the formation of α-hydroxyglutarate and glutamate, a cyclic pathway (a succinate-glycine cycle), which involves γ, ô-dioxovalerate and α-hydroxy-glutarate as key intermediates, was proposed. Additional data in support of the proposed mechanism were as follows: (1) dioxovalerate was incorporated into glu-tamate in vivo as well in vitro; (2) [14C] glutamate formation from [14C] dioxo-valerate in a cell-free system was strongly inhibited by D-α-hydroxyglutarate, indicating that the hydroxy acid is an intermediate; (3) [14C] glutamate derived from [4-14C] ô-aminolevulinate was preferentially labeled at its carbon-2.
The existence of the succinate-glycine cycle was further substantiated by demon-stration of two enzyme activities, a glyoxalase system [EC 4. 4. 1. 5 and EC 3. 1. 2. 6] and D-α-hydroxyglutarate dehydrogenase in cell-free extracts. Some properties of these enzymes were described. Of the reaction steps of the proposed pathway, only the enzymatic mechanism of dioxovalerate formation from ô-aminolevulinate remains to be elucidated. The possible significance of the succinate-glycine cycle in regulating tetrapyrrole biosynthesis was discussed.View full abstractDownload PDF (1027K) -
Tadazumi KOMIYAMA, Masachika IRIE1972 Volume 71 Issue 6 Pages 973-980
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1) Ribonuclease from Rhizopus sp. (RNase Rh) [EC 2. 7. 7. 17] was found to be inhibited competitively by various kinds of nucleotides. The inhibitory effect of the nucleotides having the phosphate group at the 2'-position of ribose increased in the order of U<C<G<A. The inhibitory effect of adenine nucleotides increased in the order of 5'<3'<2' at pH 5.0.
2) Using the difference spectrum caused by the binding of 2'-AMP and enzyme, one mole of 2'-AMP, a competitive inhibitor, was found to bind with the enzyme at pH 4.5.
3) Kinetic parameters, Km and Vmax of RNase Rh were obtained using 3', 5'-ApA as substrate at various pH's. From the pKm-, log Vmax-pH profiles, pKa of a dis-sociable group of free enzyme was estimated to be 6.0. Based on this value, the possibility of the presence of histidine residue in the active site of RNase Rh was discussed.
4) Photooxidation of RNase Rh was studied to obtain the information on the nature of active site of the enzyme. The effect of pH on the photoinactivation rate indicated the involvement of a group having pKa of 6.2 in the active site. The value coincided with the pKa value of the functional group detected by kinetic studies.
5) Amino acid analysis of photoinactivated RNase Rh having 0.6% activity showed that two histidine residues had been destroyed and only about 0.5 residues of tryp-tophan and methionine had been also destroyed.
6) From the results obtained above, it was concluded that one, possibly two moles of histidine residues are important for the RNase activity and one of them has a pKa of 6.0.View full abstractDownload PDF (659K) -
Shoshi MUTO, Ikuzo URITANI1972 Volume 71 Issue 6 Pages 981-985
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe sedimentation behaviour of sweet potato glucose 6-phosphate dehydrogenase [D-glucose-6-phosphate: NADP+ oxidoreductase, EC 1. 1. 1. 49] was studied on sucrose density gradient centrifugation in the presence and absence of NADP+, and/or G6P (glucose 6-phosphate).
The sedimentation coefficient was 6.1 S in the absence of both NADP+ and G6P and was not affected by either ionic strength or pH.
In the presence of 0.1μM NADP+ or more, the sedimetation coefficient was 8.9 S at pH 8.0. In the presence of excess NADP+ (0.2mM), the sedimentation coef-ficient was 8.9 S at pH 8.0 or 8.9, but 6.3 S at pH 6.9. Ionic strength did not affect the sedimentation at pH 8.0.
The s value decreased from 8.4 to 6.1 S, with increase in the concentration of G6P (from 0.025 to 1mM), in the presence of excess NADP+ and this change in the s valve was affected by ionic strength.
In the presence of 0.1mM G6P, the s value was in the range of 6.1 to 6.9S, depending on the NADP+ concentration (2 to 200μM).View full abstractDownload PDF (404K) -
III. Recombination of Ca2+ Ion to EDTA-treated HemocyaninNobuo MAKINO1972 Volume 71 Issue 6 Pages 987-991
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSBinding of Ca2+ ion by calcium-depleted Dolabella hemocyanin was studied by means of equilibrium dialysis and H+ ion titration. It was inferred from the analysis of the data that H+ ion competes with Ca2+ ion for the binding sites. The mole of the Ca2+ ion binding sites in hemocyanin was 1.7 per minimum molecular unit (27, 900g protein containing one g-atom copper). The dissociation constants for Ca2+ and H+ ions were 2.5×10-4 and 5.6×10-7M, respectively.
The refractivity index for a solution of EDTA-treated hemocyanin was decreased by addition of Ca2+ ion, and the volume change was calculated from the decrement in refractivity to be + 110ml per 27, 900g protein, according to Ikegami's equation (l).View full abstractDownload PDF (383K) -
IV. Electrophoretic and Ultracentrifugal Approach to the Monomer-Dimer EquilibriumKunio YAGI, Nobuko OHISHI1972 Volume 71 Issue 6 Pages 993-998
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. D-Amino acid oxidase [D-amino acid: O2 oxidoreductase (deaminatiilg), EC 1. 4. 3. 3] holoenzyme migrated as a single band in zone electrophoresis on an agarose plate at several pH values from 5.5 to 9.5. The isoelectric point was found at pH 6.24.
2. In disc electrophoresis in polyacrylamide gel, the holoenzyme migrated also as a single band at pH 8.9, but separated into two bands at pH 8.2, both of which showed the enzymatic activity without the addition of the coenzyme, FAD.
3. In the experiments of isoelectric focusing, two bands were detected in both the holoenzyme and the apoenzyme.
4. Ultracentrifugal analysis indicated the occurrence of monomer and dimer of the holoenzyme. It was also indicated that the monomer-dimer equilibrium shifted towards monomer formation by the lowering of pH, temperature, or both of the solution and towards dimer formation as the holoenzyme was mixed with benzoate, a substrate-substitute.View full abstractDownload PDF (2918K) -
Tosiki NISIZAWA, Hiroshi SUZUKI, Kazutosi NISIZAWA1972 Volume 71 Issue 6 Pages 999-1007
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSFormation of cellulase [EC 3. 2. 1. 4] in washed mycelia of Trichoderma viride induced by sophorose was competitively repressed by glucose. Pyruvate also showed a similar repressive effect.
Glucose repressed the formation of constitutive enzymes such a β-glucosidase [EC 3. 2. 1. 21], xylanase [EC 3. 2. 1. 8] and amylase [EC 3. 2. 1. 1] but had little or no effect on formation of protease or acid phosphatase [EC 3. 1. 3. 2], which also seemed to be constitutive enzymes.
The inhibition by glucose was compared with those by actinomycin D and puromycin. The former resembled that by puromycin, but differed considerably from that by actinomycin D in extent and in the period required for complete ces-sation of cellulase formation after its addition. Moreover, glucose was still inhibitory when added 60 min after addition of actinomycin D by which time, further synthesis of mRNA specific for cellulase appeared to have ceased. These data suggest that catabolite repression of inductive cellulase formation in T. viride occurs mainly at the translational level of the cellulase protein.View full abstractDownload PDF (684K) -
Hiroko KIMURA, Midori YAMASHITA1972 Volume 71 Issue 6 Pages 1009-1014
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe microsomal and soluble glucose-6-phosphate dehydrogenase [D-glucose-6-phosphate: NADP oxidoreductase, EC 1. 1. 1. 49] (G6PD) in rat liver were identified by electro-phoresis and an immunological procedure. No cross immunological reaction was observed between the two. The soluble G6PD demonstrated a considerable change in response to various physiological conditions as reported, while the microsomal enzyme showed no change under any of the conditions examined. The microsomal G6PD increased during fetal development and was greatly enhanced at birth and then gradually decreased to the adult level. The microsomal enzyme in regenerating liver decreased at the 2nd day after partial hepatectomy and increased at the 5th day and returned to the normal level at the 14th day. The microsomal enzyme was not significantly found in ascites hepatoma.View full abstractDownload PDF (1733K) -
I. Metabolic Functions of NAD- and NADP-linked Malic Enzymes in Escherichia coliTadashi MURAI, Masanobu TOKUSHIGE, Jun NAGAI, Hirohiko KATSUKI1972 Volume 71 Issue 6 Pages 1015-1028
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSIn order to elucidate the metabolic functions of NAD- and NADP- requiring two malic enzymes in Escherichia coil W, various factors controlling the enzyme syntheses and metabolic flow of C4-dicarboxylic acids in the cell were studied.
The NAD-requiring malic enzyme (NAD-enzyme) [EC 1. 1. 1. 38 and 39] was repressed by glucose and induced by malate. The addition of glucose to a malate-containing medium caused a suppression of the enzyme level, but it was overcome by increasing the concentration of malate. On the other hand, the NADP-requiring malic enzyme (NADP-enzyme) [EC 1. 1. 1. 40] was repressed not only by glucose, but also by glycerol, lactate, and acetate in decreasing order of magnitude. Since the reactions to yield acetyl-CoA from the above three compounds via pyruvate are actually irreversible in vivo, acetyl-CoA or acetate was presumed to have a close relation to the repression of the enzyme. However, the concentration of acetyl-CoA in the cell had no correlation with the level of NADP-enzyme and increasing con-centrations of acetate did not exert any marked repression. Although pyruvate exhibited no appreciable repression by itself, combination of pyruvate and acetate exerted a marked repression of the enzyme. In addition, this was found to be the case also with a pyruvate dehydrogenase [EC 1. 2. 4. 1]-less mutant of E. coli. There-fore, the effect of pyruvate was presumed not to be due to conversion of pyruvate into acetyl-CoA or acetate. These results indicate that NAD-enzyme undergoes an induction by malate and NADP-enzyme a concerted repression by acetate and pyru-vate, besides the repression of both enzymes by glucose.
In resting cells of the bacterium grown on the malate medium, the radioactivity was incorporated into fatty acids from 2, 3-14C-succinate but not from 1, 4-14C-suceinate.View full abstractDownload PDF (1184K) -
Masuhisa NAKAMURA1972 Volume 71 Issue 6 Pages 1029-1041
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe biological significance of the basic amino acid residues between positions 15 and 18 of the N-terminal region of ACTH peptide was investigated by assaying the steroidogenic activities of various synthetic ACTH peptides, mainly in isolated cells of rat adrenals.
1. The tetradecapeptide Gly1-(1-14) ACTH exhibited about 1/3, 000 of the activity of the octadecapeptide (1-18) ACTH on a molar basis. The concentration-response curves of the two peptides were parallel and there was no difference in the maximum steroidogenic levels or the slopes of the curve.
2. Contrary to results in vivo, (1-18) ACTH and the carboxyl terminal-blocked amide analog, (1-18) ACTH-NH2 were equally potent when assayed in isolated adrenal cells.
3. Change from L-phenylalanine to the D-isomer at position 7 of the octadecapeptide, β-Ala1, Orn15-(1-18) ACTH-NH2 resulted in marked decrease in activity. The log-concentration response curve of β-Ala1, D-Phe7, Orn15-(1-18) ACTH-NH2 was shifted to a higher concentration range and its activity was about 3% of that of the parent L-peptide. Moreover, on simultaneous addition of both peptides, no competitive in-hibition was seen under the conditions examined.
4. The octapeptide (11-18) ACTH-NH2 potentiated ACTH-induced steroidogenesis both in vivo and in isolated adrenal cells. Kinetic experiments revealed two types of interaction, non-specific and specific, between ACTH and adrenal cells: the former involves the positive charges on the peptide and the latter is due to two portions distinguished as “active” and “binding” sites. (11-18) ACTH-NH2 decreased the amount of ACTH adsorbed on non-specific sites of adrenal cells and resulted in enhanced corticosterone production.
These results indicate that the active site of ACTH peptide is located within the first 14 amino acid residues of the N-terminal region of ACTH and that elongation with the sequence Lys-Lys-Arg-Arg at positions 15 to 18 increases the affinity of ACTH peptide for adrenal cells. The correct configuration of amino acid residues in the N-terminal region is also important for the affinity of ACTH peptide for adrenal cells.View full abstractDownload PDF (1097K) -
I. Electrophoretic StudiesKiichi IMAMURA, Takehiko TANAKA1972 Volume 71 Issue 6 Pages 1043-1051
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSIt was established that the M types of pyruvate kinase (PK) [EC 2. 7. 1. 40] in muscle and liver differed electrophoretically, the enzyme in muscle migrating rather faster than that in liver. Therefore, these enzymes were tentatively designated as M1 (skeletal muscle type-M) and M2 (liver type M), respectively. In rats, the M2-type is widely distributed in glycolytic tissues, such as liver, kidney, brain, heart, thymus, spleen, lung, adipose tissue, testis, ovary, ascites hepatoma AH-130, Walker's tumor, tumors induced by 3'-Me-DAB and cultured cells originating from hepatic cells. The M1-type is present in muscle as the only component, and in brain as the major com-ponent. The L-type is present in liver as the major component and in kidney as a minor component. Thus the M1- and L-types are only present in a few tissues with specialized physiological functions. Three unique forms of PK, M1-, M2-, and L-type, were also found in mouse and human tissues.
The electrophoretic patterns of the PK isozymes from rat tissues change greatly during differentiation and dedifferentiation. That is, the M2-type is predominant in fetal muscle, brain and liver, but during differentiation from the fetus to the adult, (1) the M2-type disappears and the M1-type becomes predominant in skeletal muscle, (2) the M2-type decreases and the L-type increases and becomes predominant in liver and (3) the M2-type decreases and the M1-type becomes predominant in brain. In contrast, in non cancerous portions of the liver of cancer-bearing animals, the L-type decreases, and the M2-type increases and becomes predominant with increased growth of the cancer, and the isozyme pattern finally changes to that of cancer cells where the M2-type is the only component. Furthermore, no PK specific for cancer cells could be detected. These results, therefore, strongly suggest that M2-type PK is the prototype of the PK isozymes, while the L- and M1-types are differentiated types.
PK in erythrocytes (R. B. C. -PK) differs electrophoretically from the M1-, M2-and L-types, separating from them and moving toward the anode rather slower than the L-type.View full abstractDownload PDF (3409K) -
Yoshiyuki ICHIKAWA, Toshio YAMANO1972 Volume 71 Issue 6 Pages 1053-1063
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe oxidation-reduction potential (E'0) of cytochrome P-450 was measured spectro-photometrically in rabbit liver microsomes and in a partially purified particle prepa-ration, and a value of -285mV was obtained in both cases for P-450 (FeIII)/P-450 (FeII. CO) in the pH range from 6 to 8. A potential of -310mV was determined for NADPH-cytochrome c reductase purified from the same source.
Xanthine oxidase [EC 1. 2. 3. 2] and hypoxanthine, added exogenously, could reduce cytochrome P-450 in liver microsomes. This artificial electron donor system could also support the microsomal hydroxylation of o-chloroaniline. However, cytochrome P-450 in the particle preparation was not reduced by the xanthine oxidase system unless a viologen dye was added. Purified ferredoxin-NADP+ reductase [EC 1. 6. 99. 4], NADPH-adrenodoxin reductase, and microsomal NADPH-cytochrome c reductase could also catalyze the reduction of cytochrome P-450 by NADPH in the particle preparation when supplemented by a viologen dye or a non-heme iron protein (fer-redoxin or adrenodoxin). The reduction of cytochrome P-450 by these reductase systems was not accompanied by the hydroxylation of o-chloro-aniline by the particle preparation.
Based on these observations, the mechanism of microsomal hydroxylation reac-tion is discussed.View full abstractDownload PDF (917K) -
Tadahiko KARASAWA, Kouichi YOSHIDA, Kiyoshi FURUKAWA, Kanoo HOSOKI1972 Volume 71 Issue 6 Pages 1065-1067
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
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Nobuo OKABE, Keiko SUYARI, Ken-ichi TOMITA1972 Volume 71 Issue 6 Pages 1069-1071
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
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Koscak MARUYAMA, Shin-ichi ABE1972 Volume 71 Issue 6 Pages 1073-1075
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
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Yoshiko NARAHASHI1972 Volume 71 Issue 6 Pages 1077-1080
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
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Khaik Cheang OO, Yew Huat LEE1972 Volume 71 Issue 6 Pages 1081-1084
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
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Hiroyasu NAKATA, Nobuo YOSHIDA, Yoshiko NARAHASHI, Shin-ichi ISHII1972 Volume 71 Issue 6 Pages 1085-1088
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
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Daisaburo FUJIMOTO, Kazuhiro IIZUKA1972 Volume 71 Issue 6 Pages 1089-1091
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
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Eiji ISHIKAWA, Tadaomi AIKAWA, Hisako MATSUTAKA1972 Volume 71 Issue 6 Pages 1093-1095
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
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Eiji ISHIKAWA, Tadaomi AIKAWA, Hisako MATSUTAKA1972 Volume 71 Issue 6 Pages 1097-1099
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
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Shinpei YAMADA, Yuji TONOMURA1972 Volume 71 Issue 6 Pages 1101-1104
Published: June 25, 1972
Released on J-STAGE: November 18, 2008
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