The protein component of scrapie‐associated fibrils is a glycosylated low molecular weight protein.
The protein component of scrapie‐associated fibrils is a glycosylated low molecular weight protein.
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痒病相关原纤维的蛋白质成分是糖基化的低分子量蛋白质。
DOI：
10.1002/j.1460-2075.1985.tb03808.x
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发表时间：
1985
期刊：
影响因子：
--
通讯作者：
K. Beyreuther
中科院分区：
文献类型：
--
作者：
G. Multhaup;H. Diringer;H. Hilmert;H. Prinz;J. Heukeshoven;K. Beyreuther
从分离自羊瘙痒症仓鼠脑的感染性羊瘙痒症相关原纤维（SAF）中提取的羊瘙痒症相关原纤维蛋白（SAF蛋白）不具有感染性。SAF-蛋白质由各种摩尔数的蛋白质组成。重量在碳水化合物含量而不是氨基酸组成上不同的糖蛋白种类。N-连接的碳水化合物链约占分子量的40 - 60%。重量SAF蛋白去糖基化的SAF-蛋白具有令人惊讶的低mol.重量约7 kd，代表约55个氨基酸残基。这种大小和化学分析表明SAF蛋白是一种淀粉样蛋白。对现有数据的最简单解释是SAF多肽很可能不是痒病病原体的一部分，但它与其他淀粉样蛋白一样，来源于宿主编码的蛋白质，不具有感染性。这表明富含SAF的组分的感染性是由于SAF蛋白的高碳水化合物含量引起的羊瘙痒病毒和SAF的共纯化。
Scrapie‐associated fibril protein (SAF‐protein) extracted from infectious scrapie‐associated fibrils (SAF) isolated from scrapie hamster brains is not infectious. SAF‐protein is composed of various mol. wt. species of glycoproteins differing in carbohydrate content rather than amino acid composition. The N‐linked carbohydrate chains represent approximately 40‐60% of the mol. wt. of SAF‐protein. The deglycosylated SAF‐protein has a surprisingly low mol. wt. of approximately 7 kd, representing approximately 55 amino acid residues. This size and chemical analyses indicate that SAF‐protein is an amyloid‐type of protein. The simplest explanation for the available data is that SAF‐polypeptide is very likely not to be part of the scrapie agent but that it is, like other amyloid proteins, derived from host‐encoded proteins and not infectious. It is suggested that the infectivity of fractions rich in SAF is due to co‐purification of scrapie virus and SAF caused by the high carbohydrate content of SAF‐protein.