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31 巻, 1 号
選択された号の論文の7件中1～7を表示しています
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坂口 和子, 赤堀 文昭, 光崎 龍子, 政岡 俊夫1987 年 31 巻 1 号 p. 1-5
発行日: 1987/02/28
公開日: 2009/03/31
ジャーナル フリーWistar Rat の血清ChE isoenzyme とChE活性値を分析することで, 性・年令に差があることを知る. 1) Wistar Rat のChE isoenzyme は, 明確に6分画されており, 分画数については, 性ならびに年令差はみられなかった. 2)分画した各 band の相対濃度比は雌では, band 6が73%と最も高い割合を示し, 次いでband 5が19%であり, この band 6および5がいわゆる main band となっていた. 次いで Sub-band としてband 3>2>1>4の順に減少する値が得られた. 一方, 雄の6W令では main band である band 5および6の相対分画濃度比はほぼ同程度であったが, 12W令になると band 5が70%と band 6 (17%) より大きな値を示していた. このように各 band の相対濃度比のうえには性差の存在することが認められた.抄録全体を表示PDF形式でダウンロード (1625K) -
和田 守史, 伊藤 喜久, 櫻林 郁之介, 河合 忠, 上村 孝, 今泉 厚1987 年 31 巻 1 号 p. 7-13
発行日: 1987/02/28
公開日: 2009/03/31
ジャーナル フリーTryptophan-poor α1-glycoprotein was initially isolated by Haupt and Heide in 1964, and designated as α1-T glycoprotein (α1-T). α1-T was originally isolated from pooled human serum, with 5 steps of chromatography, and improved by introducing affinity chromatography conjugated with anti α1-T monoclonal antibody.
The molecular weight of purified α1-T was about 77, 500 daltons determined by SDS-PAGE.
Amino acid composition were determined and was almost identical to that obtained by Schwick. Partial amino acid sequence was-Glu-Ser-Leu-Leu-Asn-His-Phe-Leu-Tyr-Glu……which did not show any homology to that reported with all existing proteins.
Anti α1-T rabbit serum and anti α1-T monoclonal antibody were prepared with purified α1-T.抄録全体を表示PDF形式でダウンロード (4585K) -
前川 真人, 須藤 加代子, 菅野 剛史1987 年 31 巻 1 号 p. 15-18
発行日: 1987/02/28
公開日: 2009/03/31
ジャーナル フリーWe examined two families with silent type hypocholinesterasemia, by using electrophoretic analysis and immunological method.
One case had trace amount of normal cholinesterase (ChE; EC 3.1.1.8.) activity. By immunological method, production of ChE protein was observed in the case. A part of the protein was seemed to show ChE activity. The case was suspected to be caused by a disturbance of polymerization, because C4 band was weak by electrophoretic analysis. Another case had neither ChE activity nor production of ChE protein. The former was homozygote of silent gene type II, and the latter, homozygote of silent gene type I.
Therefore, heterogeneity of the silent gene is very rich in Japan and variation is demonstrated to be in some steps of ChE production.抄録全体を表示PDF形式でダウンロード (2089K) -
芝 紀代子, 長 裕子1987 年 31 巻 1 号 p. 19-26
発行日: 1987/02/28
公開日: 2009/03/31
ジャーナル フリーVarious different stainings were tested with cellulose acetate membrane as a supporting medium, in order to study their sensitivities for staining protein fractions at very low concentrations. The pigment Acid violet 17 was found to be most sensitive, requiring only a sample size of 1μl for a sample with a total protein concentration of 200mg/dl and 4μl for a total protein concentration of 50mg/dl. Acid violet 17 staining was approximately 10 times more sensitive than Ponceau 3R staining, and since cerebrospinal fluid may be analysed in the unconcentrated form at this sensitivity, it promises to be clinically useful. Acid violet 17 staining is easy to perform, and gave advantages over other stainings in terms of sensitivity, rapidity, and economy, hence we believe Acid violet 17 staining provides a very suitable method for routine analysis.抄録全体を表示PDF形式でダウンロード (3494K) -
Glucosylated albumin を中心として西村 敏郎, 牧野 義彰, 金丸 育恵, 紺野 邦夫1987 年 31 巻 1 号 p. 27-32
発行日: 1987/02/28
公開日: 2009/03/31
ジャーナル フリーThe nonenzymatic glucosylation reaction occurs in various proteins of the body, particularly in diabetic subjects. Glucosylated human albumin was prepared by incubating albumin with glucose in the presence or absence of sodium cyanoborohydride (NaCNBH3) for 2 weeks at 37°C. We prepared a newly boronate affinity chromatography system by connecting 3-aminophenyl boronic acid hemisulfate with CNBr-activated Sepharose 4B. Using this system, synthetic glucosylated albumin, normal serumm and diabetic were applied to this Boronate Sepharose column. Pure glucosylated protein was separated from them. Glucosylated albumin levels to the total albumin were 49% in the synthetic nonreduced glucosylated albumin. Glucosylated protein levels to the total protein were determined in 5 of the diabetic subjects and ranged from 10.4% to 15.7% (mean±SD 11.2±2.0). Glucosylated protein levels ranged from 5.6 to 8.0 (mean±SD 6.9±0.9) in 5 of the normal subjects. Glucosylated protein values were significantly greater in diabetic subjects than in normal subjects. The reduced glucosylated albumin moved more rapidly than nonglucosylated albumin and nonreduced glucosylated albumin on agarose electrophoresis. However, the reduced glucosylated albumin on polyacrylamide electrophoresis moved a little more rapidly than the other albumins.
A male rabbit was immunized with human reduced glucosylated albumin. On day 120 blood was obtained for our studies. To document the presence of antibodies, we used the Ouchterlony method and confirmed an antibody against reduced glucosylated albumin.抄録全体を表示PDF形式でダウンロード (2284K) -
山口 稽子, 浅川 英男1987 年 31 巻 1 号 p. 33-36
発行日: 1987/02/28
公開日: 2009/03/31
ジャーナル フリーColloidal gold was used to detect extremely small amount of proteins electrotransferred on nitrocellulose membrane after sodium dodecyl sulfate polyacrylamide gel electrophoresis. Clearly deep wine-red bands of proteins were obtained by using 0.002∼0.005% colloidal gold solution stabilized with Tween 20. The sensitivity was in the same range as silver staining of polyacrylamide gel and enough to detect nanogram order of proteins applied on the gel.抄録全体を表示PDF形式でダウンロード (4058K) -
島尾 和男1987 年 31 巻 1 号 p. 37-39
発行日: 1987/02/28
公開日: 2009/03/31
ジャーナル フリーPDF形式でダウンロード (2163K)
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