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纯化小鼠干扰素的异质性。

Heterogeneity of purified mouse interferons.

作者信息

Knight E

出版信息

J Biol Chem. 1975 Jun 10;250(11):4139-44.

PMID:236313
Abstract

A procedure for obtaining highly purified stable interferon from mouse L cells is described. Interferon with a specific activity of 2.5 times 10-8 reference units/mg of protein is composed of 10 to 11 polypeptides. They differ in their molecular size as determined by electrophoresis on polyacrylamide gels containing sodium dodecyl sulfate. The molecular weight range is estimated to be from the smallest at 20, 000 to the largest at 32, 000. At least six of the polypeptides are glycoproteins and each of the polypeptides can be obtained as an apparent homogeneous entity and each has interferon activity.

摘要

本文描述了一种从小鼠L细胞中获得高度纯化的稳定干扰素的方法。比活性为2.5×10⁻⁸参考单位/毫克蛋白质的干扰素由10至11种多肽组成。通过在含有十二烷基硫酸钠的聚丙烯酰胺凝胶上进行电泳测定,它们的分子大小不同。分子量范围估计从最小的20,000到最大的32,000。至少六种多肽是糖蛋白,并且每种多肽都可以作为明显的单一实体获得,并且每种都具有干扰素活性。

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