人血清和脑脊液中与14kda凝集素抗原性相关的寡克隆β-半乳糖苷结合免疫球蛋白:纯化和表征

Raymonde Joubert-Caron , Michel Caron , Pascal Bochet , Ahmed Chadli , Pierre Delaporte , Edmond Schuller , Dominique Bladier
{"title":"人血清和脑脊液中与14kda凝集素抗原性相关的寡克隆β-半乳糖苷结合免疫球蛋白:纯化和表征","authors":"Raymonde Joubert-Caron ,&nbsp;Michel Caron ,&nbsp;Pascal Bochet ,&nbsp;Ahmed Chadli ,&nbsp;Pierre Delaporte ,&nbsp;Edmond Schuller ,&nbsp;Dominique Bladier","doi":"10.1016/0020-711X(94)90111-2","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. An antiserum raised against a 14kDa β-galactoside specific lectin from human brain (HBL14) was used to probe blots from samples of serum and cerebrospinal fluid. The only HBL14-immunoreactive material detected was heavy and light chains of a β-galactoside-binding IgG fraction (lectin-like IgG).</p></span></li><li><span>2.</span><span><p>2. Lectin-like IgG, as well as IgG Fab fragments, compete with HBL14 for binding either to anti-HBL14 antibody or to a lactosyl polyacrylamide-based copolymer.</p></span></li><li><span>3.</span><span><p>3. Purification of lectin-like IgG was obtained by affinity chromatography on immobilized rabbit anti-lectin immunoglobulins. The carbohydrate-binding specificity of the purified molecules was restricted to β-Gal-containing structures and close to the HBL14 one.</p></span></li></ul></div>","PeriodicalId":13733,"journal":{"name":"International Journal of Biochemistry","volume":"26 6","pages":"Pages 813-823"},"PeriodicalIF":0.0000,"publicationDate":"1994-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711X(94)90111-2","citationCount":"8","resultStr":"{\"title\":\"Oligoclonal β-galactoside-binding immunoglobulins antigenically related to 14kda lectin in human serum and cerebrospinal fluid: Purification and characterization\",\"authors\":\"Raymonde Joubert-Caron ,&nbsp;Michel Caron ,&nbsp;Pascal Bochet ,&nbsp;Ahmed Chadli ,&nbsp;Pierre Delaporte ,&nbsp;Edmond Schuller ,&nbsp;Dominique Bladier\",\"doi\":\"10.1016/0020-711X(94)90111-2\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. An antiserum raised against a 14kDa β-galactoside specific lectin from human brain (HBL14) was used to probe blots from samples of serum and cerebrospinal fluid. The only HBL14-immunoreactive material detected was heavy and light chains of a β-galactoside-binding IgG fraction (lectin-like IgG).</p></span></li><li><span>2.</span><span><p>2. Lectin-like IgG, as well as IgG Fab fragments, compete with HBL14 for binding either to anti-HBL14 antibody or to a lactosyl polyacrylamide-based copolymer.</p></span></li><li><span>3.</span><span><p>3. Purification of lectin-like IgG was obtained by affinity chromatography on immobilized rabbit anti-lectin immunoglobulins. The carbohydrate-binding specificity of the purified molecules was restricted to β-Gal-containing structures and close to the HBL14 one.</p></span></li></ul></div>\",\"PeriodicalId\":13733,\"journal\":{\"name\":\"International Journal of Biochemistry\",\"volume\":\"26 6\",\"pages\":\"Pages 813-823\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-06-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0020-711X(94)90111-2\",\"citationCount\":\"8\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"International Journal of Biochemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0020711X94901112\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"International Journal of Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0020711X94901112","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 8

摘要

1.1. 一种抗人脑中14kDa β-半乳糖苷特异性凝集素(HBL14)的抗血清用于检测血清和脑脊液样品的印迹。唯一检测到的hbl14免疫反应物质是β-半乳糖苷结合IgG片段(凝集素样IgG)的重链和轻链。凝集素样IgG和IgG Fab片段与HBL14竞争,与抗HBL14抗体或基于乳糖基聚丙烯酰胺的共聚物结合。利用兔抗凝集素免疫球蛋白亲和层析纯化凝集素样IgG。纯化分子的碳水化合物结合特异性仅限于含有β- gal的结构,与HBL14结构接近。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Oligoclonal β-galactoside-binding immunoglobulins antigenically related to 14kda lectin in human serum and cerebrospinal fluid: Purification and characterization

  • 1.

    1. An antiserum raised against a 14kDa β-galactoside specific lectin from human brain (HBL14) was used to probe blots from samples of serum and cerebrospinal fluid. The only HBL14-immunoreactive material detected was heavy and light chains of a β-galactoside-binding IgG fraction (lectin-like IgG).

  • 2.

    2. Lectin-like IgG, as well as IgG Fab fragments, compete with HBL14 for binding either to anti-HBL14 antibody or to a lactosyl polyacrylamide-based copolymer.

  • 3.

    3. Purification of lectin-like IgG was obtained by affinity chromatography on immobilized rabbit anti-lectin immunoglobulins. The carbohydrate-binding specificity of the purified molecules was restricted to β-Gal-containing structures and close to the HBL14 one.

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:604180095
Book学术官方微信