SEIBUTSU BUTSURI KAGAKU
Online ISSN : 1349-9785
Print ISSN : 0031-9082
ISSN-L : 0031-9082
Volume 34, Issue 4
Displaying 1-7 of 7 articles from this issue
  • A comparison with Ca2+-dependent 30KDa lactose-binding Xenopus laevis skin lectin
    Kazuo Nitta, Yutaka Terasaki, Masahiro Hosono, Yasuhiro Kanno, Koya Ku ...
    1990 Volume 34 Issue 4 Pages 185-193
    Published: August 15, 1990
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    A lectin of 47KDa from skin of Xenopus laevis was purified by combination of chromatography and electrophoresis, Sephadex G-75 gel filtration, DEAE-cellulose chromatography, nondenaturating polyacrylamide gel electrophoresis and DEAE 5 PW chromatography. The lectin agglutinates human erythrocytes without showing any specificity for A, B and O blood groups. A lectin of 30KDa purified from the same starting materials by galactose-Sepharose connected to lactose-Sepharose column affinity chromatography and nondenaturating polyacrylamide gel electrophoresis preferentially agglutinated blood group A erythrocytes. Both 47KDa lectin- and 30KDa lectin-induced blood group A erythrocyte agglutination reactions were inhibited by lactulose, lactose and blood group glycoproteins. Since two lectins from the same starting materials were prepared by the different methods, purification methods and their order may affect molecular form and cell or sugar specificity of the purified lectin.
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  • Kiyotaka Fujita, Ikunosuke Sakurabayashi, Tadashi Kawai, Mutsuko Kusan ...
    1990 Volume 34 Issue 4 Pages 195-199
    Published: August 15, 1990
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    Abnormal IgM-λ type pyroglobulin from a patient with Waldenstrom's macroglobulinemia was studied. Factors influencing pyroprecipitability were examined through experiments designed to study some of the immunochemical properties of IgM-λ type pyroglobulin.
    The inhibition of pyroprecipitation by 2-mercaptoethanol was not seen. When the patient's IgM was purified, pyroprecipitability attenuated. Pyroprecipitability was markedly potentiated by adding normal purified IgG and complements. The possibility exists that these proteins (IgG and complements) act as precipitator at the pyroprecipitability.
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  • Taizo Hayashi, Keiko Hirokawa, Toru Watanabe, Yasutaka Kaneda, Noboru ...
    1990 Volume 34 Issue 4 Pages 201-205
    Published: August 15, 1990
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    CK-activities and CK-isoenzymes were measured in serum of the patients with prostatic cancer and benign prostatic hyperplasia. Both groups were consist of each 20 cases, and there were no significant differences in the age of both group. CK-BB increased more apparently in the cancer group than in the hyperplasia, especially in the stage D of cancer. No significant differences were found in total CK activities, CK-MB, and CK-MM between the cancer and the hyperplasia. CK-BB positively correlated with ACP and PAP in the hyperplasia, while there were no correlation in the cancer. It was a interesting finding that CK-BB significantly correlated with γ-Sm in the cancer but not in the hyperplasia. CK-BB also might be considered as a marker of the prostatic cancer.
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  • Kazuo Umetsu, Isao Yuasa, Tsuneo Suzuki
    1990 Volume 34 Issue 4 Pages 207-210
    Published: August 15, 1990
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    A method for removing of unnecessary antibodies was developed. Allo A lectin-Sepharose 4B and its binding serum glycoproteins were crosslinked by the dimethyl suberimidate. The antibodies on the market were purified by affinity chromatography on glycoproteins-allo A-Sepharose. By the method, anti-α1-antitrypsin, anti-hemopexin and anti-transferrin were obtained from the eluted fraction, and anti-retinol binding protein was obtained from the nonretarded fraction. On the other hand, anti-factor I and anti-Gc-globulin were obtained from both fractions. The method proved to be excellent for removing unnecessary antibodies from so called monospecific antibody on the market.
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  • Kiitiro Sitizyo, Takashi Takeuchi, Minoru Suzuki, Toshiyuki Saito
    1990 Volume 34 Issue 4 Pages 211-216
    Published: August 15, 1990
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    Serum of embryos, 1 day old chicks and 36 day old chicks were used in this experiment. α-lipoprotein and β-lipoprotein were separated by agarose gel electrophoresis. The composition of lipids in α- and β-lipoproteins were analyzed by silica gel chromatography. The ratios of total lipid to total protein were correlated with the mobility of α-lipoprotein on the celulose acetate electrophoresis. α-lipoproteins (chick embryo serum) with the higher mobility contained a larger amount of I+II fraction of phospholipid and IV fraction of cholesterolester. It is concluded that mobility of α-lipoprotein is influenced by the concentration of phospholipid and fatty acid composition of cholesterolester.
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  • Kiyotaka Fujita, Ikunosuke Sakurabayashi, Akihiko Yamaguchi, Mutsuko K ...
    1990 Volume 34 Issue 4 Pages 217-221
    Published: August 15, 1990
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    A human polyclonal IgG which bound to bilirubin was present in the serum of a patient with disseminated eosinophilic collagen disease. Applying the modified Michaëlsson procedure for bilirubin analysis, the bilirubin in the patient's serum was shown conflicting results, which was high in the direct bilirubin than in the total bilirubin. By bilirubin staining after electrophoresis and Protein A affinity chromatography, we showed that the bilirubin in the patient's serum was bound to the patient's IgG. This bilirubin-IgG complex was not completely dissociated by treatment with strong acid or 2-mercaptoethanol. The purified IgG from the patient's serum in which bilirubin-IgG complex had disappeared on recovery, was able to recombine with standard bilirubin. Indirect bilirubin which bound to the patient's IgG was measured as direct bilirubin applying the modified Michaëllson procedure.
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  • Matsuo Sato, Yahei Koseki, Mitsutaka Yoshida, Kei Furiya
    1990 Volume 34 Issue 4 Pages 223-229
    Published: August 15, 1990
    Released on J-STAGE: March 31, 2009
    JOURNAL FREE ACCESS
    By means of cellogel membrane electrophoresis, anomal alkaline phosphatase (orthophosphoric monoester phosphohydrolase, EC 3.1.3.1, ALP) isozyme showing a broad band of major activity from post β-globulin to pre γ-globulin region was found in the serum obtained from a patient with rheumatoid arthritis. The major component of serum ALP obtained from the patient found to be 19s fraction by gel filtration. The obtained macromolecular ALP was confirmed to be ALP-linked with IgM (kappa chain) by enzymoimmunoelectrophoresis. Furthermore, the isolated IgM from the ALP-linked IgM interacts with the tested all ALP isozymes (liver/bone, placenta and intestine) by immunofixation technique, suggesting that the IgM recognizes multivalent epitopes of the ALP. According to enzymatic properties, the ALP-linked IgM which might be originated from placental ALP. Because, the susceptibilities for heat and amino acids of the ALP-linked IgM were similar to that of placental ALP.
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