[兔骨骼肌nad -激酶的四级结构]。

Ukrains'kyi biokhimichnyi zhurnal Pub Date : 1977-07-01
I D Insarova, V I Telepneva
{"title":"[兔骨骼肌nad -激酶的四级结构]。","authors":"I D Insarova,&nbsp;V I Telepneva","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The quaternary structure and some kinetic properties were studied for NAD-kinase from the rabbit skeletal muscles. The molecular weight of the 150-300-fold purified enzymic preparation was determined by separation in the Sephadex G-200 thin layer, by means of Sephadex G-200 column gel-filtration and by the method of electrophoresis in the gradient of polyacrylamide gel concentration. Some molecular forms of NAD-kinase with a molecular weight of 31000-305000 are found in the enzymic preparation and possibility to change from one form to another is shown. On the basis of the established quaternary structure and complex kinetic characteristics of the enzyme a conclusion is drawn on the existence of the rabbit skeletal muscle NAD-kinase as an equilibrium system of the oligomeric forms possessing different catalytic activity and consisting of different combinations of subunits with a molecular weight of 31000.</p>","PeriodicalId":23396,"journal":{"name":"Ukrains'kyi biokhimichnyi zhurnal","volume":"49 4","pages":"124-9"},"PeriodicalIF":0.0000,"publicationDate":"1977-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[Quaternary structure of NAD-kinase from rabbit skeletal muscles].\",\"authors\":\"I D Insarova,&nbsp;V I Telepneva\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The quaternary structure and some kinetic properties were studied for NAD-kinase from the rabbit skeletal muscles. The molecular weight of the 150-300-fold purified enzymic preparation was determined by separation in the Sephadex G-200 thin layer, by means of Sephadex G-200 column gel-filtration and by the method of electrophoresis in the gradient of polyacrylamide gel concentration. Some molecular forms of NAD-kinase with a molecular weight of 31000-305000 are found in the enzymic preparation and possibility to change from one form to another is shown. On the basis of the established quaternary structure and complex kinetic characteristics of the enzyme a conclusion is drawn on the existence of the rabbit skeletal muscle NAD-kinase as an equilibrium system of the oligomeric forms possessing different catalytic activity and consisting of different combinations of subunits with a molecular weight of 31000.</p>\",\"PeriodicalId\":23396,\"journal\":{\"name\":\"Ukrains'kyi biokhimichnyi zhurnal\",\"volume\":\"49 4\",\"pages\":\"124-9\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1977-07-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Ukrains'kyi biokhimichnyi zhurnal\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Ukrains'kyi biokhimichnyi zhurnal","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

摘要

研究了兔骨骼肌nad -激酶的季元结构和部分动力学性质。采用Sephadex G-200薄层分离、Sephadex G-200柱凝胶过滤、聚丙烯酰胺凝胶浓度梯度电泳等方法测定150-300倍纯化酶制剂的分子量。在酶制剂中发现了一些分子量为31000-305000的nadk分子形式,并显示了从一种形式转变为另一种形式的可能性。根据已建立的酶的四级元结构和复杂的动力学特征,得出兔骨骼肌nad -激酶是一个由不同亚基组合组成的具有不同催化活性的低聚物平衡系统,分子量为31000。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
[Quaternary structure of NAD-kinase from rabbit skeletal muscles].

The quaternary structure and some kinetic properties were studied for NAD-kinase from the rabbit skeletal muscles. The molecular weight of the 150-300-fold purified enzymic preparation was determined by separation in the Sephadex G-200 thin layer, by means of Sephadex G-200 column gel-filtration and by the method of electrophoresis in the gradient of polyacrylamide gel concentration. Some molecular forms of NAD-kinase with a molecular weight of 31000-305000 are found in the enzymic preparation and possibility to change from one form to another is shown. On the basis of the established quaternary structure and complex kinetic characteristics of the enzyme a conclusion is drawn on the existence of the rabbit skeletal muscle NAD-kinase as an equilibrium system of the oligomeric forms possessing different catalytic activity and consisting of different combinations of subunits with a molecular weight of 31000.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
[Use of vitamins for correction of the functional state of cytochrome P450 systems in experimental allergic encephalomyelitis]. [Influence of oxidative stress on the level of genes expression Tgfb1 and Hgf in rat liver upon long-term gastric hypochlorhydria and administration of multiprobiotic Symbiter]. [Mathematical modeling of calcium homeostasis in smooth muscle cells while activity of plasma membrane calcium pump is modulated]. [Antitoxic and antioxidant effects of N-stearoylethanolamin in the content of nanocomposite complex with doxorubicin in organs of mice with Lewis carcinoma]. [Influence of Ca2+ on kinetic parameters of pancreatic acinar mitochondria in situ respiration].
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1