首页    期刊浏览 2024年11月28日 星期四
登录注册

文章基本信息

  • 标题:Physicochemical characterization of six monoclonal cryoimmunoglobulins: possible basis for cold-dependent insolubility
  • 本地全文:下载
  • 作者:C R Middaugh ; B Gerber-Jenson ; A Hurvitz
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1978
  • 卷号:75
  • 期号:7
  • 页码:3440-3444
  • DOI:10.1073/pnas.75.7.3440
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:The physical and chemical properties of five human and one canine monoclonal cryoimmunoglobulin have been compared. By many criteria, the proteins cannot be distinguished from the noncryoglobulin reference proteins analyzed in parallel; however, certain hydrodynamic and spectroscopic properties of the proteins indicate that cryoimmunoglobulins differ in tertiary structure relative to their cold-soluble counterparts. These differences seem to favor low-temperature-induced association between cryoglobulin molecules as an immediate consequence of increased intermolecular ionic or van der Waals forces. No evidence was found for the formation of cold-dependent antigen-antibody complexes or the ubiquitous presence of low-temperature-dependent conformation changes as a component of cryoprecipitation. Rather, the anomalous solution behavior of monoclonal cryoimmunoglobulins can be considered a direct result of the individual solubility properties of these proteins.
国家哲学社会科学文献中心版权所有