Butler N A, Lee E Y, Whelan W J
Carbohydr Res. 1977 May;55:73-82. doi: 10.1016/s0008-6215(00)84444-4.
It has long been claimed, but frequently disputed, that part of the glycogen in rat liver is insoluble in 10% trichloroacetic acid, and a physiological significance was ascribed to the existence of the two pools of glycogen, desmo-glycogen, the insoluble form, and lyo-glycogen, the soluble component. Desmo-glycogen was thought to owe its acid insolubility to a covalent binding to protein. Recent claims that glycogen, similarly insoluble in acid, can be synthesized in vitro have renewed the interest in desmo-glycogen. We have obtained trichloroacetic acid-insoluble glycogen from rat liver and find that, despite subjecting the glycogen to proteolysis, peptide material remains in close association with the glycogen through a number of purification procedures and is freed from glycogen only by enzymic decomposition of the latter. The tenacity with which the glycogen and peptide material remain in association with each other is suggestive of the occurrence of protein-bound glycogen.
长期以来，人们一直声称，但也经常受到争议，大鼠肝脏中的部分糖原不溶于10%的三氯乙酸，并且认为糖原的两个池（不可溶形式的结合糖原和可溶成分的溶解糖原）的存在具有生理意义。结合糖原被认为其酸不溶性归因于与蛋白质的共价结合。最近有声称称，类似地不溶于酸的糖原可以在体外合成，这重新引发了人们对结合糖原的兴趣。我们从大鼠肝脏中获得了不溶于三氯乙酸的糖原，发现尽管对糖原进行了蛋白水解，但在一系列纯化过程中，肽物质仍与糖原紧密结合，只有通过糖原的酶促分解才能使其与糖原分离。糖原和肽物质相互紧密结合的韧性表明存在蛋白质结合的糖原。
