Isolation procedures for thyroglobulin: effects of phenylmethanesulfonyl fluoride and freezing.

B J van der Walt, P P van Jaarsveld
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Abstract

The presence of fast-migrating, low-molecular weight components in normal rat thyroglobulin, iodine-poor rat thyroglobulin and normal bovine thyroglobulin was investigated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. When normal and iodine-poor rat thyroglobulin were extracted in the presence of phenylmethanesulfonyl fluoride, a serine protease inhibitor, very few components migrating faster than the 12S half-molecule were found. In normal bovine thyroglobulin no effect of the protease inhibitor on the formation of fast-moving components was found; however, prior freezing of the glands greatly influenced the presence of these components. Thyroglobulin obtained from bovine glands without any prior freezing, contained no noncovalently-bound band migrating faster than 12S.

甲状腺球蛋白的分离方法:苯甲磺酰氟和冷冻的影响。
用聚丙烯酰胺凝胶电泳法研究了正常大鼠甲状腺球蛋白、缺碘大鼠甲状腺球蛋白和正常牛甲状腺球蛋白中快速迁移的低分子量组分的存在。在丝氨酸蛋白酶抑制剂苯甲磺酰氟的存在下提取正常和缺碘大鼠甲状腺球蛋白时,发现很少有组分迁移速度比12S半分子快。在正常牛甲状腺球蛋白中,蛋白酶抑制剂对快速运动成分的形成没有影响;然而,事先冷冻腺体极大地影响了这些成分的存在。从牛腺体中获得的甲状腺球蛋白未经任何事先冷冻,不含非共价结合带,迁移速度超过12S。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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