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Mitsuo MORIMOTO
1966 Volume 42 Issue 3 Pages
189-192
Published: 1966
Released on J-STAGE: September 12, 2006
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Shin-ichiro IHARA
1966 Volume 42 Issue 3 Pages
193-197
Published: 1966
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Setsuo SAITO
1966 Volume 42 Issue 3 Pages
198-200
Published: 1966
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Kaneyuki YAMAMOTO, Ryosuke HOTAKA
1966 Volume 42 Issue 3 Pages
201-203
Published: 1966
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Hitoshi KUMANO-GO
1966 Volume 42 Issue 3 Pages
204-209
Published: 1966
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Ikuo KIMURA
1966 Volume 42 Issue 3 Pages
210-212
Published: 1966
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Yasuyuki IMAI, Kiyoshi ISÉKI
1966 Volume 42 Issue 3 Pages
213-216
Published: 1966
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Kiyoshi ISÉKI
1966 Volume 42 Issue 3 Pages
217-220
Published: 1966
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Shotaro TANAKA
1966 Volume 42 Issue 3 Pages
221-224
Published: 1966
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R. J. MIHALEK
1966 Volume 42 Issue 3 Pages
225-230
Published: 1966
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Akira ASADA
1966 Volume 42 Issue 3 Pages
231-236
Published: 1966
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R. J. MIHALEK
1966 Volume 42 Issue 3 Pages
237-239
Published: 1966
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Nobuhiko TATSUUMA
1966 Volume 42 Issue 3 Pages
239-242
Published: 1966
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O. P. RAI
1966 Volume 42 Issue 3 Pages
243-246
Published: 1966
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Shûichirô MAEDA
1966 Volume 42 Issue 3 Pages
247-251
Published: 1966
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Nobuyuki IKEDA, Masao NAGASAWA, Shinzo WATANABE
1966 Volume 42 Issue 3 Pages
252-257
Published: 1966
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Takashi TSUJI
1966 Volume 42 Issue 3 Pages
258-263
Published: 1966
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Nobuo KOBATAKE, Tadao KAMEI
1966 Volume 42 Issue 3 Pages
264-269
Published: 1966
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Sajiro MAKINO, Takao AYA, Tatsuro IKEUCHI, Shoichi KASAHARA
1966 Volume 42 Issue 3 Pages
270-274
Published: 1966
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Ten patients with aseptic meningitis were subjected to chromosomal studies based on the cultured leucocytes, and the incidence of chromosome breaks in the ten cases was compared with that of controls. Though several types of chromosome aberrations, low in frequency, are observed, the most common and frequent aberration in leucocytes from patients is the chromatid-type breakage. Data at hand indicate that the difference in breakage frequency is not striking between patient and control specimens.
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Seiichi OHKUMA, Shigenori IKEMOTO, Chitose MIYAUCHI, Tanemoto FURUHATA
1966 Volume 42 Issue 3 Pages
275-279
Published: 1966
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Treatment of human erythrocytes with crystalline chymotrypsin in a low concentration of 0.0732mg/ml, results in decrease of the Fy
a activity of their erythrocytes and simultaneous liberation of a sialoglycopeptide with the Fy
a activity.
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II Antibody Formation of Mononuclear Phagocyte and its Transfer Agent
Susumu MITSUHASHI
1966 Volume 42 Issue 3 Pages
280-284
Published: 1966
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These reports from this and other laboratories strongly suggest that the mononuclear phagocytes play a role not only in taking up antigen but also in turning it into template of RNA nature. According to the presence of cell-bound antibody in immune mononuclear phagocytes and the formation of antibody by treatment with the transfer agent derived from immune cells, it is concluded that the mononuclear phagocytes constitute an additional cell line to plasma cellular and lymphoreticular cells lines responsible for antibody formation.
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XIV The Enzymatic Conversion of Fetal Hemoglobin into a Possible Precursor of Biliverdin by Heme α-Methenyl Oxygenase. I
Fumio KUMA
1966 Volume 42 Issue 3 Pages
285-290
Published: 1966
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1) The enzymatic degradation of fetal hemoglobin was studied by the use of chromatographically purified hemoglobin F as the substrate. 2) Hemoglobin F
II is active as a substrate of Table I. Inhibitors of enzyme reaction. The reaction mixture consisted of 1.0ml. of partially purified enzyme, 1.0ml. of boiled liver extract, 0.3ml. of 1×10-2M methemoglobin FII and 0.4ml. of inhibitor solution dissolved in water and 0.4ml. of 0.1M phosphate buffer, in a final volume of 3.0ml. heme α-methenyl oxygenase either in the absence or in the presence of haptoglobin. 3) Inhibitors of ferrous iron and those of -SH groups inhibit the reaction. 4) The degradation process seems to be analogous to that of hemoglobin A-haptoglobin complex, myoglobin and pyridine-hemichromogen, and the further investigations are now in progress.
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XIV The Enzymatic Conversion of Fetal Hemoglobin into a Possible Precursor of Biliverdin by Heme α-Methenyl Oxygenase. II
Fumio KUMA
1966 Volume 42 Issue 3 Pages
291-294
Published: 1966
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1) The final reaction product obtained by the enzymatic conversion of hemoglobin F
II due to heme α-methenyl oxygenase was characterized. 2) The product was failed to crystallize at the present time, however, the structure of heme part seemed to be quite analogous to 656mμ-absorbing substance, the product obtained by the degradation of pyridine-hemichromogen by the same enzyme. 3) The enzymatic conversion of hemoglobin F will be catalyzed by heme α-methenyl oxygenase as same as hemoglobin A-haptoglobin complex, myoglobin and pyridine-hemichromogen, and further investigations on the reaction mechanism are now in progress.
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Hideo SUGITA, Kyoko OKIMOTO, Setsuro EBASHI
1966 Volume 42 Issue 3 Pages
295-298
Published: 1966
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