Purification and characterization of four components of rat caseins

Masaaki Hirose , Toshio Kato , Kenji Omori , Makoto Takeuchi , Masaaki Yoshikawa , Ryuzo Sasaki , Hideo Chiba
{"title":"Purification and characterization of four components of rat caseins","authors":"Masaaki Hirose ,&nbsp;Toshio Kato ,&nbsp;Kenji Omori ,&nbsp;Makoto Takeuchi ,&nbsp;Masaaki Yoshikawa ,&nbsp;Ryuzo Sasaki ,&nbsp;Hideo Chiba","doi":"10.1016/0005-2795(81)90127-6","DOIUrl":null,"url":null,"abstract":"<div><p>Rat casein components (C1-, C3A-, C3B- and C4-casein) were extensively purified from rat milk, and the properties of these proteins were compared with those of other caseins including rat C2-casein. C1-casein was precipitated by a low concentration of CaCl<sub>2</sub> (1.5 mM). Both C3A- and C3B-casein were less sensitive to Ca<sup>2+</sup> than were C1- and C2-casein, and the presence of 20 mM CaCl<sub>2</sub> was required at 37°C for their precipitation. C4-casein was absolutely insensitive to Ca<sup>2+</sup>. This protein exhibited the ability to stabilize all of the other rat casein components against Ca<sup>2+</sup>-dependent precipitation. In addition, C4-casein contained sialic acid, galactose and <span><math><mtext>N-</mtext><mtext>acetylgalactosamine</mtext></math></span>. Therefore, C4-casein appears to be a bovine ϰ-casein-like protein.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1981-12-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90127-6","citationCount":"5","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Protein Structure","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0005279581901276","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 5

Abstract

Rat casein components (C1-, C3A-, C3B- and C4-casein) were extensively purified from rat milk, and the properties of these proteins were compared with those of other caseins including rat C2-casein. C1-casein was precipitated by a low concentration of CaCl2 (1.5 mM). Both C3A- and C3B-casein were less sensitive to Ca2+ than were C1- and C2-casein, and the presence of 20 mM CaCl2 was required at 37°C for their precipitation. C4-casein was absolutely insensitive to Ca2+. This protein exhibited the ability to stabilize all of the other rat casein components against Ca2+-dependent precipitation. In addition, C4-casein contained sialic acid, galactose and N-acetylgalactosamine. Therefore, C4-casein appears to be a bovine ϰ-casein-like protein.

大鼠酪蛋白四种成分的纯化及性质研究
从大鼠乳汁中广泛纯化大鼠酪蛋白组分(C1-、C3A-、C3B-和c4 -酪蛋白),并将这些蛋白与其他酪蛋白(包括大鼠c2 -酪蛋白)的性质进行比较。低浓度CaCl2 (1.5 mM)沉淀c1 -酪蛋白。C3A-和c3b -酪蛋白对Ca2+的敏感性都低于C1-和c2 -酪蛋白,在37℃条件下需要20 mM的CaCl2才能沉淀。c4 -酪蛋白对Ca2+完全不敏感。该蛋白表现出稳定所有其他大鼠酪蛋白成分对抗Ca2+依赖性沉淀的能力。此外,c4 -酪蛋白还含有唾液酸、半乳糖和n -乙酰半乳糖胺。因此,c4 -酪蛋白似乎是牛ϰ-casein-like蛋白。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
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