正常人类晶状体和白内障中重分子量晶状体蛋白及水不溶性蛋白质的天冬氨酸消旋作用。
Aspartic acid racemization in heavy molecular weight crystallins and water insoluble protein from normal human lenses and cataracts.
作者信息
Masters P M, Bada J L, Zigler J S
出版信息
Proc Natl Acad Sci U S A. 1978 Mar;75(3):1204-8. doi: 10.1073/pnas.75.3.1204.
Abstract
High D/L aspartic acid ratios are observed in heavy molecular weight aggregates and in water-insoluble protein extracted from whole lenses and nuclear and cortical regions. Purified alpha-, beta-, and gamma-crystallins have low D/L ratios. Fractionation of urea-solubilized material from the water-insoluble protein yields four molecular weight classes of proteins. Fractions representing crosslinked material or apparently degraded products have high D/L ratios. Racemization within lens proteins may contribute to formation of the water-insoluble fraction seen in aging lenses and cataracts.
摘要
在重分子量聚集体以及从整个晶状体、核区和皮质区提取的水不溶性蛋白质中观察到高D/L天冬氨酸比率。纯化的α-、β-和γ-晶状体蛋白具有低D/L比率。从不溶性蛋白质中对尿素可溶物质进行分级分离可得到四类分子量的蛋白质。代表交联物质或明显降解产物的级分具有高D/L比率。晶状体蛋白中的消旋作用可能有助于形成在老化晶状体和白内障中所见的水不溶性部分。
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