女子大生の減量意識と健康 ―運動意欲（2）―

We studied the consciousness about weight reduction behavior, dietary habits and motivation to do sports of young females by using a self-report questionnaire survey. The subjects were 386 female college students （fiscal 2007, Grade 1, 18.6±0.6 years old） in Nishinomiya district. Although their BMIs were almost within normal range（ 20.2±2.0）, 84% of female students had a desire to get slimmer. Most of female students were aware of the necessity of daily exercise, and recognized that the amount of their exercise had been inadequate or unsatisfactory so far

Biochemical studies on chick embryo during incubation (Agricultural Chemistry)

孵卵中の卵白のシアル酸およびトリプシン阻害活性の変化を追求した。シアル酸濃度は日と共に徐々に増加し, インヒビター活性は, 最初減少したのち増加し, それ以後は変化しなかった。孵卵数日にして形成される漿尿膜(CAM)は, 強いシアリダーゼ活性を有し, 卵白のシアロタンパク質であるオボムチンやオボムコイドからシアル酸を遊離させた。またCAM自身もシアル酸を有し, 自らもシアル酸を遊離させる。微生物由来のシアリダーゼで処理したCAMは非常に強いシアリダーゼ活性を示したが, これは加えたシアリダーゼが膜と強く結合するものと考えられる。シアロタンパク質とCAMの結合が, オボムコイドの示すトリプシン阻害活性をもって間接的に, ^Iによる標識で直接的に検討された。用いたオボムコイド, オボムチン共に脱シアル酸処理をしたCAMとよく結合し, 逆に脱シアル酸処理したタンパク質は, そのままのCAMとよく結合した。The change of sialic acid content and trypsin inhibitory activity of chicken egg white during incubation were studied. The sialic acid concentration of egg white slightly increased during incubation, indicating the absorption of sialo-proteins of egg white into embryo occurred later than that of others. In early period of incubation, trypsin inhibitory activity rapidly and extensively decreased and after this period, trypsin inhibitory activity was kept at approximately constant level. Neuraminidase (sialidase) of chorioallantoic membrane (CAM) was able to release the endogenous sialic acid and showed the strong activity toward exogenously added ovomucoid and ovomucin. When neuraminidase was mixed with CAM in a buffer, sialic acid at the membrane surface was removed. Added neuraminidase remained bound at the surface of CAM despite of sufficient washing and shows strong activity on sialo-proteins. The experiments for CAM-sialo-protein binding showed that desialylated proteins (desialylated ovomucoid and ovomucin) bound to native CAM in greater amount than to desialylated CAM. Further, it was found that native sialo-proteins (native ovomucoid and ovomucin) bound to desialylated CAM rather than native CAM. ^I-labelled sialo-proteins were prepared and used in these binding experiments

Studies on the neuraminidase from chick chorioallantoic membranes (Agricultural Chemistry)

孵卵17日目の鶏胚の漿尿膜(CAM)よりシアロ糖タンパク質をリチウム3,5-ジョードサルチル酸(LIS)やドデシル硫酸(SDS)を用いて可溶化した。LISによって可溶化されたタンパク質は, 微生物由来のシアリターゼによって加水分解されてシアル酸を遊離した。このことはCAM自体が膜シアリダーゼの基質になっている可能性を示唆している。SDSによって可溶化されたタンパク質は, 酵素の一般的阻害剤であるSDSを完全に除去することが難かしく, 加水分解されなかった。デオキシコール酸を用いて, CAMよりシアリダーゼを可溶化し, ゲル滬過とCM-Sephadex C-50によるイオン交換クロマトグラフィーによって部分精製した。可溶化した酵素はCAMより単離したタンパク質, オボムコイド, ムチン, フエツイン, コロミン酸, シアリルラクトーズなどを基質として, その性質を検討した。最適pHは4.3で60℃以上の加熱で急に失活した。コロミン酸とフエツインに対してKmやVmax値を求め, また各種カチオンの効果も検討した。The sialoglycoproteins were extracted from the chorioallantoic membranes (CAM) of 17 days-old chick embryo using lithium 3,5-diiodosalicylate (LIS) and sodium dodecyl sulfate (SDS). The sialoglycoprotein prepared from CAM with LIS was hydrolyzed by bacterial neuraminidase accompanied with the release of sialic acid. However, the sialoglycoprotein extracted by SDS from membranes was not hydrolyzed becuase of the existence of SDS which was a strong inhibitor of the enzyme. The solubilization of the neuraminidase (N-acetylneuraminylhydrolase, E. C. 3. 2. 1. 18) from the chorioallantoic membranes was carried out with the following solution : 0.1 M sodium phosphate buffer, pH 7.0,0.1 M KCl, 25% glycerol, 1 mM 2-mercaptoethanol, 0.5% deoxycholic acid sodium salt. Solubilized enzyme was partially purified by the gel filtration (Sephadex G-75) and the ion exchange chromatography (CM-Sephadex C-50). Neuraminidase activities of the intact CAM and solubilized enzyme from CAM were measured using sialoglycoproteins from CAM, chicken ovomucoid, mucin, fetuin, colominic acid, sialyllactose and ganglioside as substrate. The pH optimum was at 4.3 and a marked loss of enzyme activity was observed by heating at 60℃ and above for 60 min. Km and Vmax values were determined for colominic acid and fetuin. Though Ca^ did not affect the enzyme activity, Cu^ and Hg^ inhibited the activity extensively