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Volume 62 (1967)
- Issue 6 Pages 633-
- Issue 5 Pages 509-
- Issue 4 Pages 401-
- Issue 3 Pages 287-
- Issue 2 Pages 141-
- Issue 1 Pages 1-
Volume 62, Issue 5
Displaying 1-18 of 18 articles from this issue
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MASACHIKA IRIE1967 Volume 62 Issue 5 Pages 509-518
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESS1. A ribonuclease, (RNase M)[EC 2.7.7.17 ribonucleate nucleotido-2'-transferase (cyclizing)] was isolated from “Molsin” (Aspergillus saitoi). RNase M was purified about 125 fold by means of column chromatography using IRC-50, phospho-cellulose, DEAE-cellulose and Sephadex G-75.
2. RNase M is very similar in molecular weight to RNase T2 from Asp. ogzae.
3. RNase M has a base specificity similar to that of RNase T2 and releases adenylic acid more rapidly than the other nucleotides. However, RNase M is different from RNase T2 in the more precise base specificity.
4. RNase M is different from RNase T2 in the pH optimum as examined with RNA and U-cyclic-p as substrates.
5. The enzyme is inhibited markedly by Cu++, Zn++, Hg++ and Cd++ and less stable against heat treatment than RNase A or T1.View full abstractDownload PDF (3088K) -
III. Dehydrogenative Polymerization of Coniferyl Alcohol by PeroxidaseYuzo Nozu1967 Volume 62 Issue 5 Pages 519-530
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESS1. Dehydrogenative polymerization product (DHP) was obtained from coniferyl alcohol by the action of purified bamboo shoot peroxidase [EC 1.11.1.7] and found to give similar properties to that of native lignin except that it had a lower molecular weight (approx. 1, 000).
2. Two methods for determination of the rate of DHP formation were described, namely spectrophotometric measurements of the rate of disappearance of coniferyl alcohol and the formation of DHP.
3. Not only bamboo shoot peroxidase but also wheat germ and horseradish peroxidases were found to form DHP, indicating that plant peroxidase generally participates in the formation of DHP.
4. The rate of DHP formation was dependent on the concentrations of peroxidase, hydrogen peroxide and coniferyl alcohol. The disappearance of coniferyl alcohol in the peroxidatic reaction was inhibited by KCN, while the polymerization step was not. These results indicated that hydrogen peroxide and peroxidase are essential for dehydrogenation of coniferyl alcohol while the subsequent polymerization process occurs nonenzymatically.
5. The reactivities of peroxidase with coniferyl alcohol analogs were studied and the essential groups in the molecule of substrate for dehydrogenation and polymerization were confirmed to be a free phenolic OH group and a double bond in the side chain.
6. Attempts to increase the molecular weight of DHP formed in the enzymatic reaction were unsuccessful.
7. Based on these results, the mechanism of formation of DHP and its relation to lignification were discussed.View full abstractDownload PDF (1454K) -
II. The Reaction of N, N'-Polymethylene-bis (iodoacetamide) with Cysteine and Rabbit Muscle AldolaseHITOSHI OZAWA1967 Volume 62 Issue 5 Pages 531-536
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESS1. Several N, N'-polymethylene-bis (iodoacetamide) were synthesized and their reaction with cysteine was investigated.
2. Rabbit muscle aldolase [EC 4.1.2.13] was treated with N, N'-polymethylene-bis (iodoacetamide). When a high concentration of the enzyme and an enough amount of the brigding reagent were used, insoluble protein with an appreciable enzymatic activity was obtained in a yield of 50%.
3. When the reaction with aldolase was carried out using a dilute enzyme solution and limited amounts of bridging reagents, all the enzyme protein remained soluble. The sedimentation coefficient of the major peak was the same as that of native aldolase at pH7.5, showing that the extent of inter-molecular bridging reaction was small. The content of S-carboxymethylcysteine of the preparation was about 6 moles per mole of aldolase. The sedimentation coefficients of the acid dissociated aldorase and of the bridged aldorase were 1.6S and 2.3-2.5S, respectively. Therefore, an inter-subunit bridging must have occurred during the reaction. The bridged aldolase preparation showed no tendency of stabilization towards acid, alkali and urea denaturation. Acid denatured bridged aldorase recover less enzymatic activity on neutralization than that in the case of aldolase.View full abstractDownload PDF (2398K) -
AKIO IWASHIMA, YOSHITSUGU NOSE1967 Volume 62 Issue 5 Pages 537-542
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESS1. 2-Amino-hydroxyethylthiazole (2-amino-4-methyl-5-β-hydroxyethylthiazole), an effective inhibitor for growth of the wild type E. coli cells, inhibits the biosynthesis of thiamine from hydroxyethylthiazole. A mutant of E. coli highly resistant to 2-amino-hydroxyethylthiazole has been isolated.
2. No detectable difference in the properties of the enzymes for thiamine synthesis was observed between the mutant and the parent strains.
3. Decrease in permeability of cell membrane of the mutant for 2-amino-hydroxyethylthiazole was suggested to be the mechanism for the resistance to 2-amino-hydroxyethylthiazole.View full abstractDownload PDF (931K) -
HIROSHI HASHIZUME, MASARU SHIRAKI, KAZUTOMO IMAHORI1967 Volume 62 Issue 5 Pages 543-551
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSIt was demonstrated that the pattern of circular dichroism (CD) of poly-D-glutamic acid with peaks at 222, 206 and 190mμ represented a mirror image of that of poly-L-glutamic acid. This result suggested that the three CD peaks observed for a-helical poly-glutamic acids reflect the statues of their backbone conformation. Based on this finding, attempt was made to estimate helical contents of several protein by measuring the CD amplitude at 222mμ. The results obtained were compared with those obtained by the optical rotatory dispersion. The former results were in good agreement with the latter. The CD peak observed at 280mμ for several proteins was attributed to tyrosyl residues. By comparing with the CD pattern of poly-L-tyrosine it was concluded that the band at 280mμ of proteins is due to buried tyrosyl residues. Likewise, the CD band at around 290mμ was attributed to buried tryptophanyl residues. The thermal denaturation of several proteins was studied by following the CD bands at 280 and 290mμ.View full abstractDownload PDF (1341K) -
XCVII. Metabolism of Epicoprostanol in the Japanese EelTAKAHIKO HOSHITA, SHIGEO HIROFUJI, SHOICHI ENOMOTO1967 Volume 62 Issue 5 Pages 552-557
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSEpicoprostanol-4-14C was synthesized chemically and administered intraperitoneally to Japanese eels. About 20% and 10%, respectively, of the administered radioactivity were recovered in the gall bladder bile and a liver extract after 24 hours. Taurolithocholate was identified as the major metabolite of epicoprostanol in the eel.View full abstractDownload PDF (672K) -
I. Kinetic StudieTAIBO YAMAMOTO, Yuji TONOMURA1967 Volume 62 Issue 5 Pages 558-575
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
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KATSUHIDE YUTANI, ASAKO YUTANI, TOSHIZO ISEMURA1967 Volume 62 Issue 5 Pages 576-583
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESS1.The rate of reactivation of urea-denatured bacterial α-amylase [EC 3.2.1.1] was increased by the presence of bovine serum albumin, egg albumin, casein, and disulfide interchange enzyme in reactivation medium.Gelatin and γ-globulin had no effect.Ribonuclease [EC2.7.7.16] and lysozyme [EC 3.2.1.17] acted inhibitory.
2.Polyamino acids had no significant effect on the reactivation, in spite of their characteristics, that is, acidic, basic, or neutral.Reduced carboxymethylated bovine serum albumin had no accelerating effect. These results show that the acceleration of coexisting protein is required to have some specific conformation.
3.In the absence of proteins, if urea-denatured bacterial α-amylase was very highly diluted, the extent of the reactivation was low.This suggests that the interaction among polypeptide chains of denatured protein might be necessary during the reactivation process.
4.The protein containing in the renaturation medium promotes the reformation of correct structure of the enzyme from denatured, unfolded protein.View full abstractDownload PDF (1075K) -
KAZUE OZAWA, KIICHIRO SETA, HIROSHI ARAKI, HAJIME HANDA1967 Volume 62 Issue 5 Pages 584-590
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSBrain mitochondria were found to contain 3-4 times as much K+ and 4-15 times as much Na+ as in mitochondria prepared from liver, kidney and heart.The K+ concentration in brain mitochondria was estimated to be 120 mM.This concentration of K+, when supplied in the external medium, supported maximal phosphorylation by brain mitochondria oxidizing NAD-linked substrates.
During brief ischemia, a loss of K+ and a gain in Na+ were induced in brain mitochondria.The mitochondrial K+/Na+ ratio decreased from 3.7 to 2 at a uniform rate during the first 5 minutes of ischemia. However, the Mg++ and inorganic phosphate contents remained nearly constant.
The brain mitochondrial K+ was very labile and remarkably released by repeated washing, but the K+ in the other mitochondria could not be removed by several washings.
The behavior of brain mitochondrial K+ was correlated directly with liberation of free fatty acids from mitochondrial membrane and decay of phosphorylation efficiency.
The possible relation between K
+ binding to brain mitochodria and inhibition of phosphorylation by free fatty acids is discussed.View full abstractDownload PDF (1053K) -
HISAO KATO, TOMOJI SUZUKI, KIYOSHI IKEDA, Kozo HAMAGUCHI1967 Volume 62 Issue 5 Pages 591-598
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESS1.The physicochemical properties of purified bovine kininogen-II were studied.The molecular weight was calculated to be 46, 600 from sedimentation and diffusion coefficients, 48, 600 from the Scheraga-Mandelkern relation using β=2.12×106 and 47, 000 by the Archibald method. These values are in good agreement with the value reported previously of 49, 500 from amino acid analysis. The sedimentation and diffusion coefficients extrapolated to zero concentration were found to be 3.66 S and 6.16×10-7 cm.2 sec.-1, respectively. The partial specific volume, 5, was 0.668ml./g. The intrinsic viscosity, [η] was 0.063 dl./g.at 25°C. The isoelectric point was determined by free boundary electrophoresis and found to be at pH 3.3. The electrophoretic mobility at pH 8.20 was-8.21×10-5 cm.2 sec.-1 volt-1.The frictional ratio, f/fmin., was 1.48, and the absorbancy, E1%1cm., was 6.7 at 280 mμ.
2.The gross conformations of kininogen-II and of its derivatives were investigated by measurements of optical rotatory dispersion, circular dichroism and difference spectra.Kininogen-II has a low α-helical content and possibly has the β-structure in some part of the molecule, but when kinin is released enzymatically, the content of α-helix or β-structure of the residual protein increases.When the disulfide linkages in kininogen-II were completely reduced and carboxymethylated, the resulting RCM-kininogen had a quite different conformation from those of native and dekininated proteins.View full abstractDownload PDF (1148K) -
IKUKO YANAGI, HIROMICHI OKUDA, HARUKO NAKANO, YASUMASA YAMANOUCHI, SET ...1967 Volume 62 Issue 5 Pages 599-603
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSCalcium ion is required for ACTH to exert a lipolytic action on ratepididymal adipose tissue slices.Other metal ions such as Mg++, Zn++, Cu++, Ba++ and Mn++ can not substitute for Ca++.In the adipose tissue homogenate the action of ACTH disappears and calcium ion stimulates lipolysis.Besides, ACTH increases the incorporation of calcium ion into the adipose tissue slices.All these results suggest that the lipolytic effect of ACTH might be mediated through calcium ion.View full abstractDownload PDF (586K) -
NOBUKO MIYAJIMA, JIRO KOYAMA, IKUO YAMASHINA1967 Volume 62 Issue 5 Pages 604-609
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESS1.The incorporation of 14C-glucosamine into 7S γ1-and γ2-globulins and anti-ovalbumin antibodies was investigated using slices of spleen, lung and bone marrow from guinea pigs which were hyperimmunized with ovalbumin.
2.Differences in the rate of glucosamine incorporation in the immunoglobulin subclasses from different tissues, and a higher content of anti-ovalbumin antibodies in 7S γ1-globulins than in 7S γ2-globulins were observed, results similar to those obtained from comparable experiments with 14C-amino acids.
3.Since the light chains of 7S γ-globulins significantly incorporated radiolabel, it was suggested that some glucosamine added to the medium was metabolically converted to amino acids prior to incorporation into protein in the tissue slices.View full abstractDownload PDF (729K) -
III. Purification and Properties of the Mitochondrial Enzyme from Hog Heart and Comparison with the Supernatant EnzymeKENJI AKI, KOICHI OGAWA, AKIO SHIRAI, AKIRA ICHIHARA1967 Volume 62 Issue 5 Pages 610-617
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSAn specific transaminase for valine, leucine and isoleucine with α-ketoglutarate was purified from mitochondria of hog heart and its properties were compared with those of the similar enzyme from the supernatant.The purified mitochondrial enzyme was shown to be a single protein by ultracentrifugal, electrophoretic and immunological procedures.
Its sedimentation constant, optimum pH, SH requirement and substrate specificity were similar to those of the supernatant enzyme.
However, the Km values of the mitochondrial enzyme for branched chain amino acids were one tenth of those of the supernatant enzyme, while that for α-ketoglutarate was four times larger than that of the supernatant enzyme.The Km values of the two enzymes for pyridoxal phosphate were also significantly different.A difference between the two enzymes was also shown in their stability.Thus the supernatant enzyme was more stable than the mitochondrial one on heat treatment or aging.The supernatant enzyme was eluted slightly ahead of the mitochondrial enzyme from a Sephadex G-100 column.The two enzymes have different electrophoretic mobilities on acrylamide gel plate.
These results indicate that the branched chain amino acid transaminase of hog heart mitochondria is specific for these amino acids like the supernatant enzyme, but the protein natures of the two are different.View full abstractDownload PDF (5234K) -
OSAMU MINARI, HIROKO TSUBONO, MASAKO AKIYAMA, TOSHIO SAKAGAMI1967 Volume 62 Issue 5 Pages 618-620
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
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HIROYOSHI HIDAKA, TOSHIHARU NAGATSU, KUNIO YAGI1967 Volume 62 Issue 5 Pages 621-623
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
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TSUNEO OKUYAMA, KOJI TAKIO, KOZO NARITA1967 Volume 62 Issue 5 Pages 624-626
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
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TAKASHI MURACHI, KEIKO KATO1967 Volume 62 Issue 5 Pages 627-629
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
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TOMOH MASAKI, MAKOTO ENDO, SETSURO EBASHI1967 Volume 62 Issue 5 Pages 630-632
Published: November 25, 1967
Released on J-STAGE: January 25, 2011
JOURNAL FREE ACCESSDownload PDF (3885K)
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