Simple and rapid method for determination of abemaciclib in human serum using supported liquid extraction pretreatment and LC-MS/MS analysis

学位記番号：医博甲1827

Biological activities specified by antibiotic resistance plasmids

Bacteria can display resistance to a wide spectrum of noxious agents and environmental conditions, and these properties are often mediated by genes located on extrachromosomal DNA elements called plasmids. Replication, vertical and horizontal transmission and evolution of these elements are discussed, and examples of the genes responsible for the resistance phenotypes are given. Selective forces that drive the evolution of new combinations of bacterial properties of particular importance in clinical situations are analyse

リパーゼ活性測定の簡便法開発とプーアル茶の阻害効果検討への応用

食品成分のリパーゼ活性阻害を調べるため，従来の測定法より簡便で，有色試料を用いた場合でも測定可能な測 定法（簡便法）を開発した．リパーゼの作用で生じた脂肪酸は，血清中の遊離脂肪酸測定法を用いて測定した．酵 素活性阻害の実験を行うに当たり，次の3点を検討した．①エタノールによる呈色過程への影響，②実験に用いる 酵素濃度および基質濃度の検討，③従来の中和滴定法との比較． 　また，これらの検討結果から導かれた簡便法を用いて，プーアル茶によるリパーゼ活性の阻害について検討し た．その結果，次のことがわかった． 　1．NEFA C-テストワコーの非結合型脂肪酸の測定キットにおける発色過程においてエタノールによる影響はな かった． 　2．酵素反応において生成される遊離脂肪酸量はリパーゼの酵素濃度が0.5～4.0mg/mL 場合，直線的に増加した． 　3．基質濃度を0.5% から4% に増加させるに従い，遊離脂肪酸の生成量は徐々に増加した． 　4．プーアル茶によるリパーゼ活性阻害率は中和滴定法と簡便法とに差がなかった（P＞0.05）． 　5．プーアル茶によるリパーゼ活性阻害には濃度依存性が示された． 　本実験で改良したパーゼ活性測定の簡便法は，短時間で測定ができ，かつ，有色試料でも測定でききたことか ら，今後の阻害物質検索に有効な測定法になりうると考えられた．To examine the lipase activity inhibition by food ingredients, we have developed a new enzyme activity inhibition assay.　 Fatty acids produced in this assay was measured by a kit for measuring free fatty acids in serum.　This assay was examined by the following three points: ① Effect on the coloration process with ethanol.　② Examination of enzyme concentration and substrate concentration used in the experiment.　③ Comparison with the neutralization titration method.　And these examination led us to new brief method for lipase activity assay. 　Then, we examined inhibition of lipase activity by Pu Erh tea.　As a result, the findings were as follows: 　1. Coloring process in NEFA C-Test Wako Fatty acid Measurement Kit was not affected by ethanol. 　2. The amount of free fatty acids produced in the enzymatic reaction was linearly increased in the range of enzyme concentration of 0.5 ~ 4.0mg / mL. 　3. In accordance with increasing the substrate concentration to 4% from 0.5%, the amount of free fatty acids was gradually increased. 　4. As for lipase activity inhibition rate due to Pu'er tea, there was no significant difference in the neutralization titration method and the simplified method of this experiment (P＞0.05). 　5. In the lipase activity inhibition rate due to Pu'er tea, concentration dependence was shown. 　This simple method of lipase activity measurement of this experiment could be measured in a short time.　In addition, this method could be measured even in the colored sample.　Therefore, we consider the new simplified method is an effective measuring method for the search of inhibitor

Biological activities specified by antibiotic resistance plasmids

Bacteria can display resistance to a wide spectrum of noxious agents and environmental conditions, and these properties are often mediated by genes located on extrachromosomal DNA elements called plasmids. Replication, vertical and horizontal transmission and evolution of these elements are discussed, and examples of the genes responsible for the resistance phenotypes are given. Selective forces that drive the evolution of new combinations of bacterial properties of particular importance in clinical situations are analyse

膵臓リパーゼ活性の阻害に及ぼすキトサンの影響

食物繊維が膵臓リパーゼ活性に及ぼす影響を明らかにするため，胆汁酸で乳化したオリーブ油を基質とする酵素反応にキトサン，アルギン酸ナトリウム，コンドロイチン硫酸，ペクチンを添加してリパーゼ活性阻害を調べた． また，食物繊維の添加が基質の乳化状態に及ぼす影響を明らかにするため，胆汁酸で乳化した脂肪乳濁液（乳化脂肪）にキトサン，アルギン酸ナトリウム，コンドロイチン硫酸，ペクチン添加して，①油層状態の変化，②乳化状態の変化（解乳化），③これらの食物繊維と胆汁酸の吸着率を比較した．その結果，次のことが明らかになった． 1. キトサンはリパーゼ活性を阻害した．アルギン酸ナトリウム，コンドロイチン硫酸，ペクチンは，リパーゼ活性を阻害しなかった． 2. キトサン，アルギン酸ナトリウム，コンドロイチン硫酸，ペクチンを乳化脂肪に加えると，全ての条件において短時間で水層と油状層に分離した．しかし食物繊維添加 24時間後の油層の状態はキトサンと他の食物繊維では異なっていた．また，乳化状態もキトサンを添加した場合には大きな粒子が観察された． 3. キトサンの胆汁酸吸着率は 60% で他の食物繊維は 1～2% であった． 　以上のことから，キトサンによるリパーゼ活性の阻害はキトサンが胆汁酸を吸着し基質の乳化状態が変化させたことにより生じたことが示唆された． To investigate the effects of dietary fiber on the pancreatic lipase activity, chitosan, sodium alginate, chondroitin sulfate and pectin were added to the enzyme reaction using olive oil as substrate, and the inhibitory activity was examined. 　Furthermore, to investigate the effects of dietary fiber addition on the emulsified state of the substrate, chitosan, sodium alginate, chondroitin sulfate and pectin were added to the substrate emulsified by bile acid.　We have observed the following three points: ① changes in the oil layer state, ② change of emulsified state (demulsification) , and ③ adsorption rate of bile acid in the case of addition of these dietary fiber. As a result, the following results were drawn: 1. Lipase activity was inhibited by the addition of chitosan.　The addition of sodium alginate, chondroitin sulfate and pectin did not inhibit lipase activity. 　2. The addition of dietary fiber to the substrate caused a separation into an aqueous layer and an oily layer in a short time in all conditions.　However, the substrate state 24 hours later after the fiber addition differed in chitosan and other dietary fibers.　In addition, in the case of the emulsion state after adding the chitosan, large particles were observed. 　3. The bile acid adsorption rate was 60% for bile acids and it was 1‒2% for the other dietary fibers. 　Our results suggest that the inhibition of lipase activity by chitosan is due to the changes in the emulsified state of substrate by the adsorption of bile acids

過塩素酸イオンが配位した金属錯体の合成と構造

金沢大学教養部研究課題/領域番号:X00090----354215研究期間(年度):1978出典：「過塩素酸イオンが配位した金属錯体の合成と構造」研究成果報告書　課題番号X00090----354215（KAKEN：科学研究費助成事業データベース（国立情報学研究所）） （https://kaken.nii.ac.jp/ja/grant/KAKENHI-PROJECT-X00090----354215/）を加工して作