The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
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Volume 54, Issue 2
Displaying 1-18 of 18 articles from this issue
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  • Structure of Muramidase (Lysozyme)
    I. The Effect of Guanidine Hydrochloride on Muramidase
    KOZO HAMAGUCHI, ASAKO KURONO
    1963 Volume 54 Issue 2 Pages 111-122
    Published: 1963
    Released on J-STAGE: November 18, 2008
    JOURNAL FREE ACCESS
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    In order to obtain some information about the secondary and tertiary structures of the muramidase molecule, the denaturation by guanidine hydrochloride and urea was investi-gated by following changes in optical rotation, viscosity, and ultraviolet absorption spectrum. The following observations have been made:
    1. Guanidine hydrochloride acts as a much stronger denaturing agent on muramidase than urea. The viscosity, optical rotatory properties and the difference spectrum change abruptly above 3.5M guanidine hydrochloride at 25°C.
    2. The viscosity and optical rotatory pro-perties and the difference of the molar extinction coefficient at 292mμ of muramidase above 3.5M guanidine hydrochloride change with time and the changes obey a first order reaction. The rate constants determined by the changes in viscosity, mean residue rotation and Δε at 292mμ were all the same. The rate constants were also the same with that of proton uptake of three carboxyl groups which are abnormal and exposed in the presence of guanidine hydrochloride (13).
    3. The difference spectra produced by guanidine hydrochloride below 3.2M have positive peaks at 284 and 292mμ. Comparing with the difference spectra of tryptophan produced by various concentrations of guani-dine hydrochloride, it was inferred that three or four (probably, four) tryptophan chromo-phores lie at the periphery of the native muramidase molecule. This is also supported by the observation that the increment of Δε at 292mμ per mole of guanidine hydrochloride above 5M is 1.5 times the increment below 3.2M.
    4. The difference spectra of muramidase produced by guanidine hydrochloride above 4.5M have negative peaks at 284 and 292mμ and a positive peak at 300mμ. The concentration at which the blue shift occus corresponds to the concentration at which viscosity, optical rotatory properties change. The reason why a peak appears at 300mμ is not clear. It is certain, however, that the appearance of this peak is intimately related with the change in the protein conformation.
    5. The results obtained by the present experiments and those by other investigators suggest that there is an internal fold in the muramidase molecule which contains three carboxyl groups, one tyrosyl group, and two (or three) tryptophan residues and no lysyl residue.
    The authors are indebted to Prof. T. Isemura for his encouragement. They also wish to thank Prof. M. Funatsu, Drs. K. Hayashi, A. Imanishi, Y. Momotani and T. Takagi for most helpful discussions.
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  • Substrate of the Enzymatic Reaction Concerning Liberation of Ethanolamine in Rat Ascites Hepatoma
    TAIJIRO MATSUSHIMA, MASAYORI INOUYE, KEN HIGASHI, ATSUSHI OIKAWA
    1963 Volume 54 Issue 2 Pages 123-129
    Published: 1963
    Released on J-STAGE: November 18, 2008
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    1. The ethanolamine liberating enzymatic system was also present in rat ascites hepatoma (AH 130) cells.
    2. The main precursor of free ethanolamine in AH 130 cells was identified as phos-phorylethanolamine.
    3. Alkaline phosphatase which hydrolyses phosphorylethanolamine was not inhibited at all in the presence of 50 per cent of acetone even in the case of normal liver as well as AH 130.
    4. Free phosphorylethanolamine contents of AH 130 and regenerating liver of rat were larger than that of normal rat liver.
    5. The difference between normal liver and regenerating liver or tumor cells of rat in the reaction of formation of ethanolamine was discussed from the results.
    The authors wish to thank Misses T. Miyaji and C. Iwasaki for their skilled technical assistances.
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  • Properties of Acetone Insensitive Phosphatase from Ascites Hepatoma of Rat
    MASAYORI INOUYE, KEN HIGASHI
    1963 Volume 54 Issue 2 Pages 130-137
    Published: 1963
    Released on J-STAGE: November 18, 2008
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    1. The properties of the enzymatic hydrolysis of phosphoethanolamine were examined with the enzyme partially purified from AH 130 ascites hepatoma of rat.
    2. From its pH optimum and experiments on various activators and inhibitors, it was concluded that the enzyme is the same as non-specific alkaline phosphatase.
    3. The effect of various organic solvents on the activity was investigated. It was found that the hydrolysis of phosphoethanolamine was activated by several organic solvents, but that the hydrolysis of β-glycerophosphate was markedly suppressed by all solvents examined.
    4. Partially purified alkaline phosphatases from regenerating liver and normal liver of rat behaved similarly to enzyme from hepatoma cells in the presence of acetone.
    5. The difference between normal liver, and regenerating liver and tumour cells of rat in the, reaction of formation of ethanolamine (1-3) was discussed from the results described above.
    The authors wish to thank Prof. S. Akabori of the Institute for Protein Research, Osaka University, and Prof. Y. Sakamoto of this Institute and Drs. A. Oikawa and T. Matsushima of National Cancer Center Research Institute for their continuous encouragement and sympathetic interest in this work. Thanks are also due to Miss T. Miyaji for her skilled technical assistance.
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  • Effect of Acetone on Alkaline Phosphatase Activity
    MASAYORI INOUYE
    1963 Volume 54 Issue 2 Pages 138-145
    Published: 1963
    Released on J-STAGE: November 18, 2008
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    1. The effects of acetone on the activities of alkaline phosphatase with various substrates were investigated. It was found that the activity with p-nitrophenyl phosphate (PNPP) was markedly suppressed by several organic solvents, which increased the activity with phosphoethanolamine (PE).
    2. It was shown that the same enzyme or the same active site participates in the hydrolysis of both PE and PNPP.
    3. The kinetics of the reactions with PE and PNPP were analyzed in the absence and presence of acetone. It was found that the apparent Km, Michaelis constant, was decreased by acetone with PE but was increased with PNPP.
    4. From these results, the effects of acetone on alkaline phosphatase activity are discussed.
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  • Biochemical Studies on Streptolysin S'
    II. Properties of a polypeptide Component and Its Role in the Toxin Activity
    JIRO KOYAMA
    1963 Volume 54 Issue 2 Pages 146-151
    Published: 1963
    Released on J-STAGE: November 18, 2008
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    The chemical nature of streptolysin S' was investigated with a purified toxin prepared by zone electrophoresis and DEAE-cellu-lose column chromatography described in the previous paper.
    1. The presence of a polypeptide besides oligoribonucleotides in the purified toxin was demonstrated definitely by amino acid analysis and also by the incorporation of C14-amino acids into the toxin. From the rechromatog-raphic experiment with the C14-labeled toxin, high purity of the toxin preparation was demonstrated.
    2. Amino acid analysis revealed the exis-tence of Asp, Thr, Ser, Glu, Pro, Ala, Val, Ileu, Leu, Lys, and His. A polypeptide con-tained in the toxin was probably a glutamic acid (or glutamine) and serine rich one with low content of basic amino acids.
    3. The effects of several crystalline pro-teolytic enzymes were investigated. The he-molytic activity was lost by chymotrypsin, papain, Nagarse and Pronase, but not by trypsin, as noted by former investigators.
    4. From these results, it was concluded that a polypeptide was an essential component of the toxin molecule.
    The present author wish to express his sincere thanks to Prof. F. Egami for his guidance and encouragement during this work. He also indebted to Dr. K. Takahashi and Mr. S. Horiuchi for the amino acid analysis.
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  • Biosynthesis of C14-Labelled Flavin Adenine Dinucleotide by Eremothecium ashbyii
    TOSHIHARU NAGATSU, IKUKO NAGATSU-ISHIBASHI, KUNIO YAGI
    1963 Volume 54 Issue 2 Pages 152-155
    Published: 1963
    Released on J-STAGE: November 18, 2008
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    1. C14-Labelled FAD and riboflavin were synthesized from C14-formate by Eremothecium ashbyii.
    2. The ratio of specific radioactivity of synthesized FAD to that of synthesized riboflavin was 3:1.
    3. The ratio of specific radioactivity of the riboflavin part to adenine part of FAD was 1:2.
    4. In the riboflavin part of FAD, C14 was incorporated into C(2) of the isoalloxazine nucleus, and it was supposed that C14 was also incorporated into C(2) and C(8) of adenine nucleus of FAD.
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  • The Studies on the Structure of Chicken Hemoglobin
    I. Chromatogrphic Purification of Chicken Hemoglobin
    GENJI MATSUDA, HIROSHI TAKEI
    1963 Volume 54 Issue 2 Pages 156-160
    Published: 1963
    Released on J-STAGE: November 18, 2008
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    In order to separate and purify chicken hemoglobin, the authors performed column chromatography on carboxymethylcellulose by elution with salt concentration gradient of phosphate buffer. Using the above technique, chromatographic behaviors of carbonmoxy- and oxyhemoglobin and its potassium ferricyanide-oxidized form were examined. The effects of temperature on the chromatography were also studied. The present chromatographic conditions appear to be useful for the separation and the purification of chiken hemoglobin.
    The authors wish to express their sincere thanks to Prof. T. Yoritaka of Nagasaki University, School of Medicine, for his continuous encouragement, and to Prof. K. Narita of the Institute for Protein Research, Osaka University, for his kind and helpful advice.
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  • Purification and Some Properties of Cytochromes from Aspergillus oryzae
    TATEO YAMANAKA, TSUNEKO NISHIMURA, KAZUO OKUNUKI
    1963 Volume 54 Issue 2 Pages 161-165
    Published: 1963
    Released on J-STAGE: November 18, 2008
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    Aspergillus cytochromes c and b-554 were isolated and purified from Aspergillus oryzae. Aspergillus cytochrome c has its absorption peaks at 410mμ and 526mμ in the oxidized form, and at 417mμ, 520mμ and 550mμ in the reduced form. It is different from both mammalian cytochrome c and Pseudomonas cytochrome c-551 in its reactivity with cytochrome oxidases. Aspergillus cytochrome b-554 has an absorption peak at 413mμ in the oxidized form, and peaks at 423mμ, 526mμ and 554mμ, and a shoulder at 560mμ in the reduced form.
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  • Proteolipid from Beef Heart Muscle
    II. Chemical Composition and Subcellular Distribution
    MAKOTO MURAKAMI, YOSHINORI OZAWA, SABURO FUNAHASHI
    1963 Volume 54 Issue 2 Pages 166-172
    Published: 1963
    Released on J-STAGE: November 18, 2008
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    Proteolipid was prepared from beef heart muscle by the combination of fluff formation and dialysis against chloroform-methanol (2:l, v/v), and its chemical composition and subcellular distribution were studied.
    The lipid moiety consisted of phospholipids for the most part and a small amount of triglycerides. The striking features in phos-pholipid composition are the relatively low content of lecithin and high contents of phosphatidylethanolamine, polyglycerolphos-pholipid and sphingomyelin.
    The N-terminal amino acid of the protein moiety was unitary, and was identified as aspartic acid. This result appears to indicate that the proteolipid protein is considerably homogeneous.
    The data of subcellular fractionation showed that the proteolipid is localized in mitochondria.
    We are deeply indebted to Drs. I. Hara and Y. Kawanishi, Department of Serology, Faculty of Medicine, University of Tokyo, for their invaluable advice on the protein analysis.
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  • Studies on the Chemical Structure of Colistin
    II. Amino Acid Sequence of Colistin A
    TOMOJI SUZUKI, HIROYUKI INOUYE, KAZUO FUJIKAWA, SHIGEHARU NAGASAWA
    1963 Volume 54 Issue 2 Pages 173-180
    Published: 1963
    Released on J-STAGE: November 18, 2008
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    The partial acid hydrolysate of cotistin A was fractionated by gradient column chroma-tography and fifteen compounds were obtained and their sequences were identified. Five key peptides obtained from acid hydrolysate and one peptide from enzymic hydrolysate were enough to conclude the full structure of colistin A as shown in Scheme 1 (I), that is cyclo-(γ)DAB-(α)DAB→D-Leu→L→Leu→(α)DAB→(α) DAB→Thr peptide having MOA→(α)DAB→Thr→(α)DAB side chain of which carboxyl residue was attached to α-amino group of DAB in the cycle.
    The authors wish to thank Mr. T. Yano of Banyu Pharmaceutical Co., Ltd. for a gift of commercial colistin and are indebted to Mr. S. Esaka in our laboratory for his assistance in microbiological analyses.
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  • Preparation and Some Properties of S-Poor and S-Rich Charoninsulfuric Acids
    KATSUHIRA IIDA
    1963 Volume 54 Issue 2 Pages 181-188
    Published: 1963
    Released on J-STAGE: November 18, 2008
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    Charoninsulfuric acids were extracted mildly by phenol-water mixture from mucous glands of Charonia lampas. Charoninsulfuric acids were fractionated in main two fractions; S-rich and S-poor charoninsulfuric acids. Both charoninsulfuric acids were obtained in homo-genous state. S-poor and S-rich charoninsul-furic acids contained 0.7 per cent and more than 10 per cent sulfur, respectively. S-poor charoninsulfuric acid was hydrolyzed partially by α- and β-amylases and completely by an amylase of Rhizopus or by iso-amylase in the co-operation with β-amylase. S-poor chaninsulfuric acid consists of glycogen-like structure with α-1, 6-glucosidic linkages rather than amylose-like structure. Polysaccharide part of S-rich charoninsulfuric acid consists of cellulose-like structure.
    The author wishes to express his gratitude to Prof. F. Egami for. his useful advice and Mr. S. Watanabe for his collaboration. He is indebted to Prof. J. Fukumoto of Osaka City University for a gift of amylases (α-, β-, and Rhizopus amylases) and Prof. S. Akabori of University of Osaka for a gift of a-amylase (Taka-amylase). This research was sup-ported in part by grants from the Scientific Re-search Fund of the Ministry of Education and Seikagaku-kenkyusho Ltd.
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  • The N-Terminal Amino Acid Sequences of Hemoglobin of Blue-White Dolphin (Prodelphinus coeruleo-albus)
    SHIRO KONAGAYA
    1963 Volume 54 Issue 2 Pages 189-190
    Published: 1963
    Released on J-STAGE: November 18, 2008
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  • Inositol Hexasulfate, a Non-Competitive Inhibitor of Acid Phosphatase from Wheat Bran
    YASUTOYO NAGAI, SABURO FUNAHASHI, FUJIO EGAMI
    1963 Volume 54 Issue 2 Pages 191-192
    Published: 1963
    Released on J-STAGE: November 18, 2008
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  • The N-Terminal Amino Acid Sequence of Soybean Trypsin Inhibitor
    TOKUJI IKENAKA, KAZUNORI SHIMADA, YOSHIO MATSUSHIMA
    1963 Volume 54 Issue 2 Pages 193-195
    Published: 1963
    Released on J-STAGE: November 18, 2008
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  • Effect of ATP on the Binding of N-Ethylmaleimide to SH Groups in the Active Site of Myosin ATPase
    TAKAMITSU SEKINE, MASAHIRO YAMAGUCHI
    1963 Volume 54 Issue 2 Pages 196-198
    Published: 1963
    Released on J-STAGE: November 18, 2008
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  • Effect of Cyanide on the Enzymatic Reductions of Several Osones
    KIHACHIRO UEHARA, MASAO TAKEDA
    1963 Volume 54 Issue 2 Pages 199-201
    Published: 1963
    Released on J-STAGE: November 18, 2008
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  • Grystallization of D-Amninoacid Oxidase Holo-Enzyme
    KUNIO YAGI, TAKAYUKI OZAWA
    1963 Volume 54 Issue 2 Pages 202-203
    Published: 1963
    Released on J-STAGE: November 18, 2008
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  • Crystallization of a Holo-Enzyme-Product Complex of D-Aminoacid Oxidase
    KUNIO YAGI, TAKAYUKI OZAWA
    1963 Volume 54 Issue 2 Pages 204-205
    Published: 1963
    Released on J-STAGE: November 18, 2008
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