{"title":"肌凝蛋白的旋光色散。肌凝蛋白的构象变化","authors":"Yuji Tonomura , Kazuko Sekiya , Kiichi Imamura","doi":"10.1016/0006-3002(63)91034-5","DOIUrl":null,"url":null,"abstract":"<div><p>The effect of 8% dioxane on the optical rotatory dispersion of myosin A purified by treatment with DEAE-cellulose was measured in 0.6 M KCl and at pH 7.0 and 20°. The increase in the —<em>b</em><sub>0</sub> term by 5% was followed by a gradual decrease to 0.88 of the original. The —<em>b</em><sub>0</sub> term of L<sub>1</sub>-meromyosin in 0.6 M KCl and at pH 7.0 and 20% was 575 and was unchanged by the addition of dioxane, ATP of PP<sub>1</sub>. On the other hand, the —<em>b</em><sub>0</sub> term of H<sub>2</sub>-meromyosin in 0.3 M KCl and at pH 7.0 and 20% was 263. It increased by several percent immediately after the addition of 8% dioxane and decreased gradually with time. It increased by several percent on the addition of 4 moles <em>p</em>-chloromercuribenzoate, but decreased by several percent on the addition of 8 moles <em>p</em>-chloromercuribenzoate per 10<sup>5</sup> g protein. It was also decreased by the binding of H<sub>2</sub>-meromyosin with F-actin. ATP increased the —<em>b</em><sub>0</sub> term of H<sub>2</sub>-meromyosin by several percent, though PP<sub>1</sub> decreased the term by several percent. Thus these reagents change the helical content of H<sub>2</sub>-meromyosin in ways similar to the case of myosin A. The extents of the changes in the helical content of H<sub>2</sub>-meromyosin by F-actin and ATP were, however, higher than those observed in myosin A.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1963-12-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)91034-5","citationCount":"12","resultStr":"{\"title\":\"The optical rotatory dispersion of myosin a IV. Conformational changes in meromyosins\",\"authors\":\"Yuji Tonomura , Kazuko Sekiya , Kiichi Imamura\",\"doi\":\"10.1016/0006-3002(63)91034-5\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The effect of 8% dioxane on the optical rotatory dispersion of myosin A purified by treatment with DEAE-cellulose was measured in 0.6 M KCl and at pH 7.0 and 20°. The increase in the —<em>b</em><sub>0</sub> term by 5% was followed by a gradual decrease to 0.88 of the original. The —<em>b</em><sub>0</sub> term of L<sub>1</sub>-meromyosin in 0.6 M KCl and at pH 7.0 and 20% was 575 and was unchanged by the addition of dioxane, ATP of PP<sub>1</sub>. On the other hand, the —<em>b</em><sub>0</sub> term of H<sub>2</sub>-meromyosin in 0.3 M KCl and at pH 7.0 and 20% was 263. It increased by several percent immediately after the addition of 8% dioxane and decreased gradually with time. It increased by several percent on the addition of 4 moles <em>p</em>-chloromercuribenzoate, but decreased by several percent on the addition of 8 moles <em>p</em>-chloromercuribenzoate per 10<sup>5</sup> g protein. It was also decreased by the binding of H<sub>2</sub>-meromyosin with F-actin. ATP increased the —<em>b</em><sub>0</sub> term of H<sub>2</sub>-meromyosin by several percent, though PP<sub>1</sub> decreased the term by several percent. Thus these reagents change the helical content of H<sub>2</sub>-meromyosin in ways similar to the case of myosin A. The extents of the changes in the helical content of H<sub>2</sub>-meromyosin by F-actin and ATP were, however, higher than those observed in myosin A.</p></div>\",\"PeriodicalId\":94301,\"journal\":{\"name\":\"Biochimica et biophysica acta\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1963-12-13\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0006-3002(63)91034-5\",\"citationCount\":\"12\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et biophysica acta\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0006300263910345\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et biophysica acta","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0006300263910345","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 12
摘要
在0.6 M KCl条件下,在pH 7.0和20°条件下,测定了8%二氧六环对deae -纤维素纯化的肌球蛋白A旋光性的影响。在- 0项增加5%之后,逐渐减少到原来的0.88。在0.6 M KCl和ph7.0和20%条件下,L1-meromyosin的-b0 term为575,并且随着PP1的ATP二氧六环的加入而保持不变。而在0.3 M KCl、7.0 pH和20%条件下,H2-meromyosin的-b0项为263。在加入8%二氧六环后,它立即上升几个百分点,并随着时间的推移逐渐下降。当每105g蛋白质中加入4mol对氯脲苯甲酸盐时,它增加了几个百分点,但当每105g蛋白质中加入8mol对氯脲苯甲酸盐时,它下降了几个百分点。H2-meromyosin与F-actin的结合也使其降低。ATP使h2 -肌凝蛋白的-b0期增加了几个百分点,而PP1使其减少了几个百分点。因此,这些试剂以类似于肌凝蛋白A的方式改变H2-meromyosin的螺旋含量。然而,F-actin和ATP对H2-meromyosin螺旋含量的改变程度高于在肌凝蛋白A中观察到的。
The optical rotatory dispersion of myosin a IV. Conformational changes in meromyosins
The effect of 8% dioxane on the optical rotatory dispersion of myosin A purified by treatment with DEAE-cellulose was measured in 0.6 M KCl and at pH 7.0 and 20°. The increase in the —b0 term by 5% was followed by a gradual decrease to 0.88 of the original. The —b0 term of L1-meromyosin in 0.6 M KCl and at pH 7.0 and 20% was 575 and was unchanged by the addition of dioxane, ATP of PP1. On the other hand, the —b0 term of H2-meromyosin in 0.3 M KCl and at pH 7.0 and 20% was 263. It increased by several percent immediately after the addition of 8% dioxane and decreased gradually with time. It increased by several percent on the addition of 4 moles p-chloromercuribenzoate, but decreased by several percent on the addition of 8 moles p-chloromercuribenzoate per 105 g protein. It was also decreased by the binding of H2-meromyosin with F-actin. ATP increased the —b0 term of H2-meromyosin by several percent, though PP1 decreased the term by several percent. Thus these reagents change the helical content of H2-meromyosin in ways similar to the case of myosin A. The extents of the changes in the helical content of H2-meromyosin by F-actin and ATP were, however, higher than those observed in myosin A.