Immunological studies of bovine nasal cartilage proteoglycan "link proteins".
Immunological studies of bovine nasal cartilage proteoglycan "link proteins".
复制标题
牛鼻软骨蛋白多糖“连接蛋白”的免疫学研究。
DOI：
10.1021/bi00695a012
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发表时间：
1975
期刊：
影响因子：
2.9
通讯作者：
H. Keiser
中科院分区：
文献类型：
--
作者：
H. Keiser
牛鼻软骨蛋白多糖聚集体在4 M胍中被密度梯度离心分离成蛋白多糖亚基（PGS）和糖蛋白连接（GPL）组分，后者含有透明质酸和负责聚集体形成的“连接蛋白”。先前根据免疫扩散研究得出结论，GPL具有两种抗原成分，一种是与PGS共同的，另一种是对连接蛋白特异性的。然而，在本研究中发现，PGS的抗血清（应该缺乏连接蛋白）与GPL的“亚基”和“连接”成分同时反应，而PGS片段的抗血清来自于分子的透明质酸结合部分，优先与连接成分反应。GPL的还原和烷基化导致抗GPL和抗pgs血清与其连接成分的反应被修饰。这些免疫扩散结果表明，蛋白多糖亚基和连接蛋白在免疫学上是相关的，并且提示连接蛋白可能与蛋白多糖亚基的透明质酸结合部分相同并衍生自该部分。
Bovine nasal cartilage proteoglycan aggregates are dissociated and separated by density gradient centrifugation in 4 M guanidine into proteoglycan subunit (PGS) and glycoprotein link (GPL) fractions, the latter containing hyaluronic acid and "link proteins" responsible for aggregate formation. It was previously concluded on the basis of immunodiffusion studies that GPL has two antigenic components, one in common with PGS and one specific for the link proteins. However, in the present study it was found that antisera to PGS, which should lack link proteins, reacted with both "subunit" and "link" components of GPL, and antisera to fragments of PGS derived from the hyaluronic acid-binding portion of the molecule reacted preferentially with the link component. Reduction and alkylation of GPL led to modification of the reactions of both anti-GPL and anti-PGS sera with its link component. These immunodiffusion results indicate that the proteoglycan subunit and the link proteins are immunologically related and suggest that the link proteins may be identical with and derived from the hyaluronic acid binding portion of the proteoglycan subunit.