巻号一覧
44 巻, 1 号
選択された号の論文の9件中1～9を表示しています
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NOBUO UI1957 年 44 巻 1 号 p. 1-7
発行日: 1957年
公開日: 2008/11/18
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NOBUO UI1957 年 44 巻 1 号 p. 9-10
発行日: 1957年
公開日: 2008/11/18
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II. TERMINAL AMINO ACID RESIDUESYASUO YAGI, TSUNEKO TSUJIMURA, KIMIKO SATO1957 年 44 巻 1 号 p. 11-23
発行日: 1957年
公開日: 2008/11/18
ジャーナル フリー1. Terminal amino acid residues of a crystalline invertebrate hemo-globin from Anadara inflata (Reeve) were investigated.
2. Two residues each of leucine, valine and alanine exist at the C-terminal position and glycine, valine and alanine adjacent to it.
3. At least one residue each of proline and glycine seems to be present at the N-terminal position. Small amounts of glutamic acid (or glutamine) were always found with these N-terminal amino acids, but the significance of this finding is hardly explainable at present.
4. Thus, the protein component of Anadara-hemoglobin differs remarkably from those of vertebrate hemoglobins studied so far.抄録全体を表示PDF形式でダウンロード (836K) -
I. EFFECT OF CONCENTRATION ON THE RATE OF HEAT-INACTIVATION OF ENZYMESSHIGERU NAKAYAMA, YOSHIKO KONO1957 年 44 巻 1 号 p. 25-31
発行日: 1957年
公開日: 2008/11/18
ジャーナル フリーThe influences of several factors upon heat-inactivation of sweet potato β-amylase, were studied:
1. The inactivation appeared to follow first-order kinetics with respect to time.
2. In the experimental range of pH 4 to 7, β-amylase in acetate buffer was stable in the range of about pH 5.0 to 5.8, and the most stable pH was about 5.4.
In the range of 0.01 to 0.1M of acetate buffer, the less concentrated the buffer, the more stable was βamylase.
3. The more concentrated β-amylase solution, the more stable was the enzyme. And the following apparent equation may be formu-lated concerning first-order inactivation rate constant with respect to time (k), and the stoichiometrical concentration of intact enzyme solution (Ci):
k=αCi-β
where, α and β are constants. This may suggest that the physical property of enzyme protein molecule is a function of the concentration of intact enzyme solution.
We are deeply indebted to Professors S. Akabori and K. Okunuki, Faculty of Science, Osaka University, Osaka, for much encouragement and many valuable suggestions, and to Assistant Professor S. Kawaguchi, Institute of Polytechnics, Osaka City University, Osaka, for theoretical suggestions.抄録全体を表示PDF形式でダウンロード (396K) -
TARO TACHIBANA, KAORU TAMAMUSHI, REITA TAMAMUSHI1957 年 44 巻 1 号 p. 33-45
発行日: 1957年
公開日: 2008/11/18
ジャーナル フリーThe interaction of gelatin with Pb2+ ion was investigated under various conditions by means of the polarographic method. The mecha-nism of this interaction was analysed by applying the thermodynamic method to the adsorption isotherm, together with the experimental results of the viscosity measurement of the reacting systems. The results obtained are summarized as follows:
1. The interaction is divided into two parts, the first of which corresponds to the lower concentration range and the second of which to the higher concentration range of Pb2+ ion.
2. It is concluded that Pb2+ ion interacts specifically with the dis-sociated imidazol and/or carboxyl groups of the gelatin molecule. In the second part, some kinds of physical adsorption of Pb2+ ion to the gelatin-Pb2+ ion complexes are supposed to occur.
3. In the first part of specific interaction, the value of ΔF is about -3.9 kcal./mole, and the effect of pH is large, which is in agreement with the results of the globular protein-metallic ion interaction. The value of ΔS, however, is much smaller than that obtained with the globular proteins, and that of ΔH is of small negative value.
4. The maximum number of the site available to the specific gela-tin-Pb2+ ion interaction is kept nearly constant under the various con-ditions. Especially it is independent of the dilution of gelatin, while its increase with the dilution has been reported by Breyer et al. in the case of the bovine plasma albumin-methyl orange interaction. This is supposed to be an important difference between the fibrous (and com-pletely denatured) protein and the globular (and native) protein.
After the completion of this study, one of the present authors (R. T.) had an op-portunity of making the valuable discussion with Dr. B. Breye r of the University of Sydney, to whom the present authors express their thanks for his interest in this study.抄録全体を表示PDF形式でダウンロード (755K) -
II. THE PREPARATION OF L-TRYPTOPHANSETSUJI SAKURAI1957 年 44 巻 1 号 p. 47-50
発行日: 1957年
公開日: 2008/11/18
ジャーナル フリー1. Indolepyruvic acid was prepared by hydrolysis of methyl ethoxalylindoleacetate, the condensation product of methyl indoleacetate with diethyl oxalate.
2. L-Tryptophan was obtained from indolepyruvic acid by heart muscle transaminase in an yield of 24 per cent based on the methyl indoleacetate consumed.抄録全体を表示PDF形式でダウンロード (228K) -
VIII. STUDIES ON HOG BILE ACIDS. (PART 3) SYNTHESIS OF PROGESTERONE AND DESOXYCORTICOSTERONE ACETATE FROM α-HYODESOXYCHOLIC ACIDKEN'ICHI TAKEDA, TOKUO KUBOTA, JUN'ICHI KAWANAMI1957 年 44 巻 1 号 p. 51-60
発行日: 1957年
公開日: 2008/11/18
ジャーナル フリーThe procedure for the oxidation of α-hyodesoxycholic acid (I) with N-bromosuccinimide to 3-keto-6α-hydroxycholanic acid (IIa) was reinvestigated and modified. The degradation of II by the Miescher method proceeded smoothly under protecting the C3-ketone by intro-ducing the ethylene ketal group. The C6-hydroxyl group was converted to the tosylate in order to facilitate its elimination, and 3-ethylenedioxy-6atosyloxypregnan-20-one (VI) was obtained. Introduction of the C21-acetoxyl group leading to 3-ethylenedioxy-6α-tosyloxy-21-acetoxy-pregnan-20-one (XII) was accomplished using both routes, via the 21-oxalyl acid X and via the Δ20-enol acetate VIII. Treatment of VI and XII with potassium acetate in acetic acid gave progesterone (VII) and desoxycorticosterone acetate (XIII), respectively.
The authors wish to thank Mr. Y. Matsui for the determination of the infrared absorption spectra, and Messrs. T. Ieki and K. Miyahara and Miss N. Morita for the microanalyses.抄録全体を表示PDF形式でダウンロード (625K) -
YOICHI KONDO, TADANORI KAMEYAMA, NOBUO TAMIYA1957 年 44 巻 1 号 p. 61-63
発行日: 1957年
公開日: 2008/11/18
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MICHIO MATSUHASHI1957 年 44 巻 1 号 p. 65-67
発行日: 1957年
公開日: 2008/11/18
ジャーナル フリーPDF形式でダウンロード (163K)
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