THE CORE PROTEINS OF LARGE AND SMALL INTERSTITIAL PROTEOGLYCANS FROM VARIOUS CONNECTIVE TISSUES FORM DISTINCT SUBGROUPS
THE CORE PROTEINS OF LARGE AND SMALL INTERSTITIAL PROTEOGLYCANS FROM VARIOUS CONNECTIVE TISSUES FORM DISTINCT SUBGROUPS
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DOI：
10.1042/bj2300181
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发表时间：
1985-01-01
影响因子：
4.1
通讯作者：
VOGEL, K
中科院分区：
文献类型：
--
作者：
HEINEGARD, D;BJORNEPERSSON, A;VOGEL, K
从一些结缔组织中分别分离出大的和小的蛋白多糖，并对其进行比较，以确定结构相似性的程度。这是通过酶联免疫吸附试验和胰蛋白酶消化125i标记的蛋白多糖时获得的肽模式来研究的。所有的大蛋白聚糖，即来自[牛]肌腱、巩膜、软骨和主动脉，似乎都含有透明质酸结合区域的典型结构，这两种结构都是通过酶联免疫吸附试验和该区域特有的肽含量来显示的。这些蛋白聚糖还具有蛋白质核心的其他结构特征，如免疫交叉反应性和类似的肽模式所示。此外，来自主动脉的大蛋白多糖在免疫分析和肽模式方面显示出独特结构的存在。在小的蛋白聚糖中，虽然氨基酸组成和蛋白核大小非常相似，但可以确定两组。一组由来自主动脉和软骨的小蛋白聚糖组成，具有相似的肽图，并在酶联免疫吸附试验中显示免疫交叉反应性。另一个明显不同的组由来自骨、角膜、巩膜和肌腱的小蛋白聚糖组成，它们在酶联免疫吸附试验和相似的肽模式中显示出一致性。然而，两组蛋白多糖表现出部分免疫交叉反应性。
Large and small proteoglycans were separately isolated from a number of connective tissues and compared to determine the extent of structural similarity. This was studied by enzyme-linked immunosorbent assays and by the peptide patterns obtained when 125I-labelled proteoglycans were digested with trypsin. All the large proteoglycans, i.e. from [bovine] tendon, sclera, cartilage and aorta, appear to contain the structure typical for the hyaluronic acid-binding region, both shown by enzyme-linked immunosorbent assay and by content of peptides unique for this region. These proteoglycans also share other structural features of the protein core, as indicated by immunological cross-reactivity and similar peptide patterns. The large proteoglycans from aorta in addition show the presence of unique structures both upon immunoassay and with regard to peptide pattern. Among the small proteoglycans two groups can be identified, although amino acid composition and protein core sizes are grossly similar. One group consists of the small proteoglycans from aorta and cartilage having similar peptide maps and showing immunological cross-reactivity in enzyme-linked immunosorbent assay. The other distinctly different group consists of the small proteoglycans from bone, cornea, sclera and tendon, which among them show identity in enzyme-linked immunosorbent assay and similar peptide patterns. Proteoglycans from the two groups, however, show partial immunological cross-reactivity.