Bassett E W
Prep Biochem. 1975;5(5-6):461-77. doi: 10.1080/00327487508061592.
A highly active form of wheat germ agglutinin (WGA) was isolated by affinity chromatography on a partially acid hydrolyzed chitin column after extraction of the wheat germ with 0.5 M formic acid and removal of the denatured or water insoluble WGA by dialyzing against distilled water before and after affinity chromatography. The purified preparation was found to be homogeneous by gel filtration, disc electrophoresis, and chemical analysis. It reacted readily with WGA receptors in human serum and urine, giving well-defined bands on agar gel double diffusion and electrophoresis. When chemically coupled to Sepharose the WGA was very reactive with red blood cells, WGA receptors in serum, urine and other biological fluids. The Sepharose-WGA has proven to be stable over a long period of time.
用0.5M甲酸提取小麦胚芽，在亲和层析前后分别对其进行蒸馏水透析，以去除变性或水不溶性的麦胚凝集素（WGA），然后通过在部分酸水解的几丁质柱上进行亲和层析，分离出一种高活性形式的WGA。通过凝胶过滤、圆盘电泳和化学分析发现，纯化后的制剂是均一的。它能与人血清和尿液中的WGA受体迅速反应，在琼脂凝胶双向扩散和电泳中产生清晰的条带。当与琼脂糖化学偶联时，WGA与红细胞、血清、尿液和其他生物体液中的WGA受体反应非常活跃。已证明琼脂糖-WGA在很长一段时间内是稳定的。
