巻号一覧
後続誌
32 巻 (1988)
- 6 号 p. 285-
- 5 号 p. 215-
- 4 号 p. 163-
- 3 号 p. 113-
- 2 号 p. 71-
- 1 号 p. 1-
32 巻, 4 号
選択された号の論文の6件中1～6を表示しています
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青柳 豊, 市田 文弘1988 年 32 巻 4 号 p. 163-167
発行日: 1988/08/31
公開日: 2009/03/31
ジャーナル フリーPDF形式でダウンロード (450K) -
松岡 雄治1988 年 32 巻 4 号 p. 169-175
発行日: 1988/08/31
公開日: 2009/03/31
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平野 和行1988 年 32 巻 4 号 p. 177-179
発行日: 1988/08/31
公開日: 2009/03/31
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藤井 茂, 西河 淳, 坂室 大徳, 谷口 直之1988 年 32 巻 4 号 p. 181-185
発行日: 1988/08/31
公開日: 2009/03/31
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藤田 清貴, 櫻林 郁之介, 河合 忠, 草〓 睦子, 寺邑 能実1988 年 32 巻 4 号 p. 187-195
発行日: 1988/08/31
公開日: 2009/03/31
ジャーナル フリーIn this report, we described the differences between the LDH-IgG complexes in patient's sera (ten cases) and anti-LDH5 antibody in affinity to 5'-AMP and Cibacron Blue F3G-A. LDH-IgG complexes in all cases were dissociated either by passing the patient's serum through a column containing 5'-AMP-Sepharose 4B or Blue Sepharose CL-6B-e.g., the electrophoretic LDH isoenzyme pattern for concentrated bound fraction was normal. Although the unbound fraction was devoid of LDH activity, a mixture of this fraction and normal serum had the same abnormal pattern as the patient's serum alone. However, this was not true for a mixture of anti-LDH5 antiserum and normal serum.
We propose the following hypothesis for the LDH-IgG complex formation: LDH can recognize the abnormal γ-Fab region of IgG which show similarities with the conformation of NAD+ at the NAD+ binding site of the molecule, but the affinity of the LDH molecule for immunoglobulin is much weaker than that for NADH or 5'-AMP.抄録全体を表示PDF形式でダウンロード (4507K) -
仙田 晴美, 長谷川 和子, 菅野 浩1988 年 32 巻 4 号 p. 197-202
発行日: 1988/08/31
公開日: 2009/03/31
ジャーナル フリーThe presence of 2-mercaptoethanol or dithiothreitol in the protein denaturing solution used to prepare samples for SDS-PAGE gives rise to artifacts by silver staining of the gel. Addition of iodoacetamide to the reduced protein sample prevents the appearance of artifacts. Silver staining is strengthened by the dithiothreitol treatment but weakened by subsequent treatment with iodoacetamide. High concentration of dithiothreitol also inhibited development of silver staining. These effects of iodoacetamide or high concentration of dithiothreitol were observed more pronouncedly with the silver-staining method of Merril et al.4) than of Guevara.5) Mobility of the protein having intramolecular disulfide bonds is more or less slowed down depending on the concentration of dithiothreitol used. From these results it is concluded that the most suitable concentration of dithiothreitol is in the range of 40 to 80mM from the viewpoints of sensitivity of silver staining, completion of mobility shift, and sharpness of developed protein bands.抄録全体を表示PDF形式でダウンロード (5689K)
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