Laboratorium voor Plantenbiochemie, Katholieke Universiteit Leuven, Kardinaal Mercierlaan 92, B-3030, Heverlee, Belgium.
Plant Mol Biol. 1983 Jan;2(1):33-40. doi: 10.1007/BF00187574.
The synthesis and processing of rice lectin was followed in vivo in developing rice embryos. Using labelling and pulse-chase labelling experiments, the sequence of events in the synthesis and post-translational modifications of this protein could be determined. The primary lectin product observed in vivo is a high molecular weight precursor (28 K), which is post-translationally converted to a 23 K lectin protein, and in a further step cleaved into two smaller 12 K and 10 K polypeptides. The first step of the processing of the rice lectin is a rather slow process (the precursor has a half-life of about 3 h) and resembles the so-called vectorial processing of cytoplasmically made organellar proteins. The second modification consists of a (slow) proteolytic cleavage of the basic lectin subunit into two smaller polypeptides and resembles somewhat the cleavage of some legume (storage) proteins in their protein bodies.
在发育中的水稻胚中进行了凝集素的合成和加工研究。通过标记和脉冲追踪实验，可以确定该蛋白合成和翻译后修饰的事件顺序。在体内观察到的主要凝集素产物是一种高分子量前体（28 K），它被翻译后转化为 23 K 的凝集素蛋白，并在进一步的步骤中被切割成两个较小的 12 K 和 10 K 多肽。水稻凝集素加工的第一步是一个相当缓慢的过程（前体的半衰期约为 3 小时），类似于细胞质中细胞器蛋白的向量加工。第二步修饰包括碱性凝集素亚基的（缓慢）蛋白水解切割成两个较小的多肽，这与一些豆科（储存）蛋白在其蛋白体中的切割有些相似。
