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一种将小鼠IgM转化为小的活性片段的高效方法的开发与应用。

Development and application of an efficient procedure for converting mouse IgM into small, active fragments.

作者信息

Matthew W D, Reichardt L F

出版信息

J Immunol Methods. 1982;50(3):239-53. doi: 10.1016/0022-1759(82)90162-4.

DOI:10.1016/0022-1759(82)90162-4
PMID:7097007
Abstract

A simple method is described for generating active molecules with molecular weights between 110 and 230 kilodaltons from mouse immunoglobulin M. The majority of these molecules have a 1 : 1 ratio of intact heavy and light chains. Approximately 70% of the specific IgM protein will still bind antigen after digestion with only a small decrease in binding affinity. Both anti-kappa and anti-mu chain specific antisera recognize these molecules. These low molecular weight molecules are much more efficient in immunocytochemistry and have localized antigens that could not be detected with undigested IgM.

摘要

本文描述了一种简单方法,可从小鼠免疫球蛋白M生成分子量在110至230千道尔顿之间的活性分子。这些分子中的大多数重链和轻链完整,比例为1:1。仅经过消化后,约70%的特异性IgM蛋白仍能结合抗原,且结合亲和力仅有小幅下降。抗κ链和抗μ链特异性抗血清均可识别这些分子。这些低分子量分子在免疫细胞化学中效率更高,并且能够定位未消化的IgM无法检测到的抗原。

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