Bloth B, Bergquist R
J Exp Med. 1968 Nov 1;128(5):1129-36. doi: 10.1084/jem.128.5.1129.
Thyroglobulin molecules purified in a single step procedure by gel filtration were studied in the electron microscope using the negative staining technique. The molecule had the shape of a flexible helix with two turns. Its length was about 220 A and the maximal diameter of the coiled part of the molecule was estimated to be 110 A. The pitch varied between 40 and 50 A. Thyroglobulin molecules dried in sodium tungstosilicate on a carbon film as for electron microscopy retained their hemagglutination-inhibiting activity and 19S sedimentation constant when redissolved in physiological buffer.
采用凝胶过滤一步法纯化的甲状腺球蛋白分子，利用负染色技术在电子显微镜下进行了研究。该分子呈具有两圈的柔性螺旋形状。其长度约为220埃，分子盘绕部分的最大直径估计为110埃。螺距在40至50埃之间变化。如用于电子显微镜观察那样，在碳膜上用硅钨酸钠干燥的甲状腺球蛋白分子，重新溶解于生理缓冲液后仍保留其血凝抑制活性和19S沉降常数。
