Glucosylation of human lens protein and cataractogenesis.
Glucosylation of human lens protein and cataractogenesis.
复制标题
人晶状体蛋白的糖基化和白内障发生。
DOI：
10.1016/0006-291x(79)92144-2
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发表时间：
1979
影响因子：
3.1
通讯作者：
A. Spector
中科院分区：
文献类型：
--
作者：
A. Pande;W. Garner;A. Spector
利用氚化BH4− 进行晶状体蛋白糖基化的检查。总体结果表明，每摩尔蛋白质掺入了大约 0.20 摩尔氚。使用不同程度混浊的正常和老年白内障晶状体也获得了类似的结果。此外，在源自这些晶状体的可溶性和不溶性蛋白质级分之间没有观察到 3 H掺入的差异。对从老年性白内障分离的选定多肽的研究给出了可比较的结果。从糖尿病患者晶状体中分离出的蛋白质的氚掺入量略高，平均每摩尔蛋白质含 0.27 摩尔氚。对氚化产物的分析表明，大约 50% 的掺入可能是由于其他类型化合物的减少。这些结果表明糖基化似乎不是白内障形成的主要因素。
Examination of glucosylation of lens protein was conducted utilizing tritiated BH4−. The overall results indicate that approximately 0.20 moles of tritium were incorporated per mole of protein. Similar results were obtained with normal and senile cataractous lenses with varying degrees of opacity. Furthermore no difference in the3H incorporation was observed between soluble and insoluble protein fractions derived from these lenses. Investigation of selected polypeptides isolated from the senile cataracts gave comparable results. Protein isolated from diabetic lenses had only slightly higher levels of tritium incorporation, giving an average value of 0.27 moles per mole of protein. Analyses of the tritiated products indicate that approximately 50% of the incorporation is probably due to reduction of other types of compounds. These results suggest that glucosylation does not appear to be a primary factor in cataract formation.