VITAMINS
Online ISSN : 2424-080X
Print ISSN : 0006-386X
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Volume 47, Issue 2
Displaying 1-21 of 21 articles from this issue
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  • Relationships of Electronic Spectra of Vitamin B_6-dependent Enzymes to their Structures
    Fuminori MASUGI
    Article type: Article
    1973 Volume 47 Issue 2 Pages 73-84
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_73
    JOURNAL FREE ACCESS
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    Most of vitamin B_6-dependent enzymes exhibit absorption maxima at about 420mμ assignable to the coenzyme (pyridoxal phosphate) bound to the apoenzymes. However, some B_6 enzymes have their absorption maxima at ca. 360mμ(for example, aspartate β-decarboxylase) or at ca. 330mμ(phosphorylase, and several ones show at both 420 and 360mμ which are considered to be protonated imine (and its resonance form, i.e., keto enamine) and nonprotonated imine, respectively. The species absorbing light at about 330mμ are very complicated. For example, the structure for pyridoxal phosphate bound to the apoenzyme of phosphorylase b has been recently proposed to be carbinol amine located in a hydrophobic environment. On the other hand, the 340mμ species of glutamate decarboxylase at high pH region is supposed to be a substituted aldamine. This paper summarizes the relationships of the electronic spectra of vitamin B_6-dependent enzymes to their structures and presents some discussion based on the data obtained using suitable models.
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  • Covalently Bound Flavin
    Tetsuo TORAYA
    Article type: Article
    1973 Volume 47 Issue 2 Pages 85-95
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_85
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    In most flavoproteins FAD and FMN can be readily liberated as free flavin nucleotides on denaturation of the protein. During the past decade it has been reported that a variety of plant and animal tissues also contain flavoproteins whose prosthetic groups are not extracted by acidification or boiling but require proteolytic digestion for extraction. In addition to succinate dehydrogenase, other mitochondrial enzymes such as monoamine oxidase and sarcosine dehydrogenase and Chromatium cytochrome c-552 have been shown to contain this new form of flavin, which subsequently became known as "covalently bound flavin". Recently it has been demonstrated that the covalently-bound FAD in these enzymes is attached to the peptide backbone via the 8α-position of the flavin ring system, and that the immediate substituent to 8α-position is histidine in succinate dehydrogenase in C-N bond from an imidazole N(3) to the 8α-CH_2 and cysteine in monoamine oxidase in thioether linkage. Chemical and physical studies on covalently bound flavin are briefly reviewed.
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  • Determination of Vitamin B_6 Dioctanoate and Dipalmitate in Cosmetics
    Akio NOZAWA, Tatsuya SEKINE
    Article type: Article
    1973 Volume 47 Issue 2 Pages 97-103
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_97
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    The conventional Gibbs' method for estimation of pyridoxine in cosmetic preparations has been improved in order to determine the contents of pyridoxine diacylate (PIN-DA). The sample from emulsified preparations, should be dissolved in a mixture of ethanol and chloroform (1 : 1) and if large amounts of interfering materials coexist, it must be pretreated by a chloroform extraction procedure. The sample solution thus obtained is then diluted with ethanol, the PINDA in it is reacted with 2,6-dibromoquinone chlorimide, and the absorbance at 650mμ is measured. This method was shown to be enough rapid and accurate for routine analysis of cosmetic samples.
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  • Studies on Thiaminase of the Genus Clostridium : (III) THIAMINASE PRODUCTION OF CLOSTRIDIUM BOTULINUM
    Ryoji HAYASHI, Zensaku YOSHII, Tomoyasu HARADA, Susumu KOBAYASHI, Deni ...
    Article type: Article
    1973 Volume 47 Issue 2 Pages 105-110
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_105
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    Thiaminase production together with other biological characteristics of Clostridium botulinum strains were studied. Of 52 strains studied, all 12 strains of type A, 8 of 9 strains of type B and 1 of 3 strains of type F produced thiaminase-I. As a comparison, 4 strains of Cl. sporogenes were also studied and thiaminase-I production was demonstrated among all. All of the thiaminase positive strains of Cl. botulinum were proteolytic, while the thiaminase negative strains were non-proteolytic. From these observations, it is concluded that the taxonomical relationship between proteolytic strains of Clostridium botulinum and Cl. sporogenes is proved to be closer and hence the proteolytic strains of Cl. botulinum may be registered as additional members on the list of anaerobic thiaminase bacteria.
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  • Biosynthesis of Galactosyl Riboflavin Analogues and Galactosyl Sugar Alcohols by Crystalline β-Galactosidase from Escherichia coli
    Yukio SUZUKI, Kei UCHIDA
    Article type: Article
    1973 Volume 47 Issue 2 Pages 111-119
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_111
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    Riboflavin-β-galactoside was isolated in crystalline form from the incubation mixture containing o-nitrophenyl-β-D-galactopyranoside (o-NPGa), riboflavin, and crystalline β-galactosidase from Escherichia coli, and identified as 5'-D-riboflavin-β-D-galactopyranoside. Galactosides of several riboflavin analogues, such as dichloroflavin, D-araboflavin and 6,7-dimethyl-ribolumazine, were synthesized by β-galactosidase. Moreover, it was found that sugar alcohols, pyridoxine and nucleosides were able to act as the acceptor of β-D-galactosyl residue of o-NPGa. O-β-D-Ga1actosy1-5-ribitol was isolated as powdered preparations by application of paper chromatographic procedures from the incubation mixture containing o-NPGa, ribitol and crystalline β-galactosidase, and identified from its R_F value, production of ribitol and galactose after the hydrolysis by acid or β-galactosidase, and oxidation with sodium metaperiodate. From these results, it is considered that galactosyl transfer reaction to riboflavin and its analogues is functioned by β-ga1actosidase.
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  • [title in Japanese]
    [in Japanese], [in Japanese]
    Article type: Article
    1973 Volume 47 Issue 2 Pages 121-122
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_121
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  • [title in Japanese]
    [in Japanese], [in Japanese]
    Article type: Article
    1973 Volume 47 Issue 2 Pages 122-
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_122_1
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  • [title in Japanese]
    [in Japanese], [in Japanese], [in Japanese], [in Japanese], [in Japane ...
    Article type: Article
    1973 Volume 47 Issue 2 Pages 122-123
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_122_2
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  • [title in Japanese]
    [in Japanese], [in Japanese], [in Japanese], [in Japanese]
    Article type: Article
    1973 Volume 47 Issue 2 Pages 123-
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_123
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  • [title in Japanese]
    [in Japanese]
    Article type: Article
    1973 Volume 47 Issue 2 Pages 124-
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_124_1
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  • [title in Japanese]
    [in Japanese], [in Japanese]
    Article type: Article
    1973 Volume 47 Issue 2 Pages 124-125
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_124_2
    JOURNAL FREE ACCESS
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  • [title in Japanese]
    [in Japanese], [in Japanese], [in Japanese], [in Japanese]
    Article type: Article
    1973 Volume 47 Issue 2 Pages 125-
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_125_1
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  • [title in Japanese]
    [in Japanese], [in Japanese]
    Article type: Article
    1973 Volume 47 Issue 2 Pages 125-126
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_125_2
    JOURNAL FREE ACCESS
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  • [title in Japanese]
    [in Japanese]
    Article type: Article
    1973 Volume 47 Issue 2 Pages 126-127
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_126
    JOURNAL FREE ACCESS
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  • [title in Japanese]
    [in Japanese], [in Japanese]
    Article type: Article
    1973 Volume 47 Issue 2 Pages 127-128
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_127
    JOURNAL FREE ACCESS
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  • [title in Japanese]
    [in Japanese], [in Japanese]
    Article type: Article
    1973 Volume 47 Issue 2 Pages 128-
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_128_1
    JOURNAL FREE ACCESS
    Download PDF (185K)
  • [title in Japanese]
    [in Japanese], [in Japanese]
    Article type: Article
    1973 Volume 47 Issue 2 Pages 128-
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_128_2
    JOURNAL FREE ACCESS
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  • [title in Japanese]
    [in Japanese], [in Japanese]
    Article type: Article
    1973 Volume 47 Issue 2 Pages 129-
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_129
    JOURNAL FREE ACCESS
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  • [title in Japanese]
    [in Japanese], [in Japanese], [in Japanese], [in Japanese]
    Article type: Article
    1973 Volume 47 Issue 2 Pages 130-
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_130_1
    JOURNAL FREE ACCESS
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  • [title in Japanese]
    [in Japanese]
    Article type: Article
    1973 Volume 47 Issue 2 Pages 130-131
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_130_2
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  • [title in Japanese]
    [in Japanese]
    Article type: Article
    1973 Volume 47 Issue 2 Pages 131-
    Published: February 25, 1973
    Released on J-STAGE: March 02, 2018
    DOIhttps://doi.org/10.20632/vso.47.2_131
    JOURNAL FREE ACCESS
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