SEIBUTSU BUTSURI KAGAKU
Online ISSN : 1349-9785
Print ISSN : 0031-9082
ISSN-L : 0031-9082
Volume 26, Issue 3
Displaying 1-13 of 13 articles from this issue
  • Hidematsu Hirai
    1982 Volume 26 Issue 3 Pages 159-161
    Published: July 31, 1982
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
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  • Ryoki Ohkawa
    1982 Volume 26 Issue 3 Pages 163-166
    Published: July 31, 1982
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
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  • Yoshikatsu Sakagishi
    1982 Volume 26 Issue 3 Pages 167-171
    Published: July 31, 1982
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
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  • Its application to the thermodynamic analysis of concanavaline A-carbohydrate interaction
    Kazusuke Takeo, Ryosuke Suzuno, Masanori Fujimoto, Akira Kuwahara, Kaz ...
    1982 Volume 26 Issue 3 Pages 173-177
    Published: July 31, 1982
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
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  • Mitsutaka Yoshida
    1982 Volume 26 Issue 3 Pages 179-182
    Published: July 31, 1982
    Released on J-STAGE: March 31, 2009
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  • Tsutomu Inoue, Hiroshi Ishizawa, Michio Iwase
    1982 Volume 26 Issue 3 Pages 183-189
    Published: July 31, 1982
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    Micro-disc electrophoresis is a powerful tool for high resolution micro-analysis of brain secreted proteins and peptides of land snail, Euhadra peliomphala.
    Micro-disc electrophoresis apparatus consists of two parts, that is, cylindrical gel electrophoresis chamber with gel tubes (50mm long, 0.8mm inside diameter) and regulated power supply with maximum voltage and current of 500V and 500μA, respectively.
    High resolution gel and buffer system for micro-disc electrophoresis is also developed.
    High resolution electrophoretic pattern of brain secreted proteins was obtained only by electrophoresis under the constant current of 40μA/tube.
    Brain specific peptide (5, 800 dalton) of Euhadra appeared only in adult brain.
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  • Mochihiko Ohashi, Tosifusa Toda, Toshiko Fujita
    1982 Volume 26 Issue 3 Pages 191-197
    Published: July 31, 1982
    Released on J-STAGE: March 31, 2009
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  • Takashi Manabe, Tsuneo Okuyama
    1982 Volume 26 Issue 3 Pages 199-204
    Published: July 31, 1982
    Released on J-STAGE: March 31, 2009
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  • Naokatu Arakaki, Yosinobu Nagao, Hideaki Hagiwara, Jinpei Yamashita, T ...
    1982 Volume 26 Issue 3 Pages 205-206
    Published: July 31, 1982
    Released on J-STAGE: March 31, 2009
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  • Jun Miyazaki, Yasuo Endo
    1982 Volume 26 Issue 3 Pages 207-211
    Published: July 31, 1982
    Released on J-STAGE: March 31, 2009
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  • Tsuyoki Kadofuku, Takeru Iijima, Tsuneo Sato
    1982 Volume 26 Issue 3 Pages 227-234
    Published: July 31, 1982
    Released on J-STAGE: March 31, 2009
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    Arginase from rat liver was separable into two isozymes (Isozyme-I and -II). These two isozymes were purified and their properties were studied. The purification procedure was composed of homogenization, heat treatment, acetone precipitation, ethanol fractionation, CM-Sepharose chromatography, isoelectric focusing, and Sephadex G-200 gel filtration.
    The purified preparation of Isozyme-I and -II were respectively homogeneous in polyacrylamide gel electrophoresis. These two isozymes were similar to each other with respect to the Km for L-arginine and the Ki's for the competitive inhibitors, L-ornithine and L-lysine. Their optimal pHs were in the range of 10.3-10.5. There was no immunological difference between the isozymes. The isoelectric points of Isozyme-I and -II were 9.3 and 9.5, respectively. All the subunits of both isozymes had a molecular weight of 40, 000 in SDS-polyacrylamide gel electrophoresis. The results of the analysis of N-terminal amino acids suggest that both isozymes are composed of different kinds of subunits.
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  • Michiko Hamato, Terufumi Sakamoto, Tokuhiko Higashi, Shuichi Kunii, Ko ...
    1982 Volume 26 Issue 3 Pages 235-242
    Published: July 31, 1982
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    Male Wistar rats (10 weeks of age) were fed on each of two kinds of high-fat diet for ten weeks, following the administration of vitamin D2 for four days. The procedure was reported to produce an atherosclerotic change within considerably short period of time.
    Serum cholesterol remarkably increased, reaching a plateau after 3 or 6 weeks of feeding, respectively. However, the amount of HDL-cholesterol decreased below normal value at the end of the second week of feeding, followed by a gradual increase up to the normal value or more. Consequently, the increased cholesterol in serum was mostly associated with lipoproteins of lower density.
    The relative amount of α-lipoprotreins changed in parallel with the amount of HDL-cholesterol. On the other hand, the amount of VLDL plus LDL or of pre β plus β-lipoproteins showed a similar behavior to that of total cholesterol in serum.
    Liver cholesterol increased continuously, reaching a level of 18-20 times more than the amount at the start of the experiment.
    The incorporation of 14C-acetate into liver cholesterol was repressed to extemely low level in the group of rats fed on the experimental diet.
    Upon the histological examination of the arterial wall of experimental animals, the accumulation of lipid and calcium was detected as early as in a couple of weeks. However, little corelation was observed between the pathological changes and the biochemical findings.
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  • Tatsuo Tozawa, Kaoru Taishi, Junko Kuwahara
    1982 Volume 26 Issue 3 Pages 243-248
    Published: July 31, 1982
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    A reliable method to identify lactate dehydrogenase linked immunoglobulin (LDH-Ig) in human serum was described in this report. By the immunoprecipitin reaction in free liquid media, a large amount of immunoprecipitate was formed. Therefore, even slight LDH activity in this precipitate could be detected and then class and type of LDH-Ig could be identified easily. We demonstrated this new method in 9 cases where the existence of LDH-Ig was suspected. By usual methods, i. e., staining LDH activity after immunoelectrophoresis, immunodiffusion or immunofixation, neither class nor type was identified on two of them, only type was identified on one of them, and both type and class were identified on the other six cases. However, both class and type of LDH-Ig could be determined in all the cases by the present method. The results show that this method is simple, quick and sensitive enough to identify LDH-Ig.
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