电火花蛋白的性质第三部分

Eberhard G. Trams, Carl J. Lauter
{"title":"电火花蛋白的性质第三部分","authors":"Eberhard G. Trams,&nbsp;Carl J. Lauter","doi":"10.1016/0926-6526(64)90007-2","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The isolation and characterization of a protein fraction from the electric organ of <em>Electrophorus electricus</em> is described. The protein was a material of relatively low molecular weight. It was soluble in water, dilute base and dilute acid and had many of the characteristics of mucoproteins.</p></span></li><li><span>2.</span><span><p>2. Analytical studies revealed the presence of galactose, <em>N</em>-acetylgalactosamine, glucuronic acid and of <em>N</em>-acetylneuraminic acid. Evidence is presented which indicated, however, that the carbohydrate constituents did not occur as a single polysaccharide moiety. The protein or polypeptide moiety apparently does not contain any of the aromatic amino acids.</p></span></li><li><span>3.</span><span><p>3. Physical studies of the isolated sialoprotein reveal marked polyanionic characteristics. Dye-binding and dye-displacement studies as measured by fluorescence quenching demonstrated that “receptor-like” function was simulated by this materiall. It was concluded, however, that this particular sialoprotein, in the form isolated, merely showed ion-exchange capabilities and lacked the high degree of specificity postulated for biological receptors.</p></span></li></ul></div>","PeriodicalId":100172,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides","volume":"83 3","pages":"Pages 296-304"},"PeriodicalIF":0.0000,"publicationDate":"1964-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6526(64)90007-2","citationCount":"5","resultStr":"{\"title\":\"Properties of electroplax protein part III\",\"authors\":\"Eberhard G. Trams,&nbsp;Carl J. Lauter\",\"doi\":\"10.1016/0926-6526(64)90007-2\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. The isolation and characterization of a protein fraction from the electric organ of <em>Electrophorus electricus</em> is described. The protein was a material of relatively low molecular weight. It was soluble in water, dilute base and dilute acid and had many of the characteristics of mucoproteins.</p></span></li><li><span>2.</span><span><p>2. Analytical studies revealed the presence of galactose, <em>N</em>-acetylgalactosamine, glucuronic acid and of <em>N</em>-acetylneuraminic acid. Evidence is presented which indicated, however, that the carbohydrate constituents did not occur as a single polysaccharide moiety. The protein or polypeptide moiety apparently does not contain any of the aromatic amino acids.</p></span></li><li><span>3.</span><span><p>3. Physical studies of the isolated sialoprotein reveal marked polyanionic characteristics. Dye-binding and dye-displacement studies as measured by fluorescence quenching demonstrated that “receptor-like” function was simulated by this materiall. It was concluded, however, that this particular sialoprotein, in the form isolated, merely showed ion-exchange capabilities and lacked the high degree of specificity postulated for biological receptors.</p></span></li></ul></div>\",\"PeriodicalId\":100172,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides\",\"volume\":\"83 3\",\"pages\":\"Pages 296-304\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-11-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6526(64)90007-2\",\"citationCount\":\"5\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926652664900072\",\"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 (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926652664900072","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 5

摘要

1.1. 描述了从电鳗的电器官中分离和表征的蛋白质组分。蛋白质是一种相对低分子量的物质。它可溶于水、稀碱和稀酸,具有粘液蛋白的许多特性。分析研究显示,其中含有半乳糖、n -乙酰半乳糖胺、葡萄糖醛酸和n -乙酰神经氨酸。然而,有证据表明,碳水化合物成分并不是作为单一的多糖部分出现的。蛋白质或多肽片段显然不含任何芳香氨基酸。分离的唾液蛋白的物理研究显示明显的多阴离子特性。通过荧光猝灭测量染料结合和染料位移的研究表明,这种材料模拟了“受体样”功能。然而,结论是,这种特殊的唾液蛋白,在分离的形式下,仅仅表现出离子交换能力,缺乏生物受体所假定的高度特异性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Properties of electroplax protein part III

  • 1.

    1. The isolation and characterization of a protein fraction from the electric organ of Electrophorus electricus is described. The protein was a material of relatively low molecular weight. It was soluble in water, dilute base and dilute acid and had many of the characteristics of mucoproteins.

  • 2.

    2. Analytical studies revealed the presence of galactose, N-acetylgalactosamine, glucuronic acid and of N-acetylneuraminic acid. Evidence is presented which indicated, however, that the carbohydrate constituents did not occur as a single polysaccharide moiety. The protein or polypeptide moiety apparently does not contain any of the aromatic amino acids.

  • 3.

    3. Physical studies of the isolated sialoprotein reveal marked polyanionic characteristics. Dye-binding and dye-displacement studies as measured by fluorescence quenching demonstrated that “receptor-like” function was simulated by this materiall. It was concluded, however, that this particular sialoprotein, in the form isolated, merely showed ion-exchange capabilities and lacked the high degree of specificity postulated for biological receptors.

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
×
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
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
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 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信