Comparison of cartilage structural glycoproteins with matrix proteins and fibronectin.
Comparison of cartilage structural glycoproteins with matrix proteins and fibronectin.
复制标题
软骨结构糖蛋白与基质蛋白和纤连蛋白的比较。
DOI：
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发表时间：
1981
期刊：
影响因子：
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通讯作者：
J. Bowness
中科院分区：
文献类型：
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作者：
J. Bowness
用4M胍从幼犬肋软骨中提取蛋白多糖和可溶性基质蛋白后，HCl处理后，不溶性含胶原的残留物已显示含有两种胶原酶抗性结构糖蛋白A和G。这些不溶性的结构糖蛋白的特征亚基已被确定溶解它们与50 mM二硫苏糖醇（DTT）在1%的十二烷基硫酸钠（SDS）和8 M尿素和比较SDS圆盘凝胶模式与那些更容易溶解的基质蛋白。三个亚基带，没有发生在凝胶中的可溶性基质蛋白被发现在溶解的材料从含胶原蛋白的残留物和结构糖蛋白。在A和G糖蛋白中均发现一条约87000道尔顿的带。另外两条谱带形成了一个间隔很近的双峰，约为30 000和27 500道尔顿，其中较低的谱带在G.尽管这些SDS凝胶带中没有一条与在相同条件下由纯纤连蛋白产生的220 000道尔顿带相对应，但一部分溶解的糖蛋白材料在显示对胶原蛋白、纤维蛋白原、肝素和血浆纤连蛋白抗体的亲和力方面与纤连蛋白相似。来自人血浆的粗纤连蛋白含有少量组分（包括约87000道尔顿中的一种），其在免疫扩散反应中与溶解的软骨结构糖蛋白的组分显示部分同一性。可溶性A与抗血浆纤连蛋白的反应比G强，可溶性基质蛋白不与抗血浆纤连蛋白反应。细胞间结构糖蛋白可能是通过选择某些存在于结缔组织和血浆中的纤连蛋白的部分裂解产物而形成的，或者组织结构糖蛋白的裂解产物存在于血浆中，与抗血浆纤连蛋白交叉反应。
After extraction of proteoglycans and soluble matrix proteins from canine puppy rib cartilage, with 4 M guanidine . HCl, the insoluble collagen-containing residue has been shown to contain two collagenase-resistant structural glycoproteins, A and G. The characteristic subunits of these insoluble structural glycoproteins have been identified by solubilizing them with 50 mM dithiothreitol (DTT) in 1% sodium dodecyl sulfate (SDS) and 8 M urea and comparing the SDS disc gel patterns with those of more readily soluble matrix proteins. Three subunit bands which did not occur in gels from the soluble matrix proteins were found in the solubilized material from both the collagen-containing residue and the structural glycoproteins. One band, of about 87 000 daltons, was found equally in both A and G glycoproteins. The other two bands formed a closely spaced doublet, of about 30 000 and 27 500 daltons, of which the lower band is present in higher concentration in G. Although none of these SDS gel bands corresponds with the 220 000 dalton band produced by pure fibronectin under the same conditions, a fraction of the solubilized glycoprotein material resembles fibronectin in showing an affinity for collagen, fibrinogen, heparin, and an antibody to plasma fibronectin. Crude fibronectin from human plasma contains minor components (including one of about 87 000 daltons) which show partial identify in immunodiffusion reactions with components of the solubilized cartilage structural glycoproteins. Solubilized A gave a stronger reaction with anti-plasma fibronectin than did G and the soluble matrix proteins have no reaction. It is possible either that the intercellular structural glycoproteins are formed by selection of some of the partial cleavage products of fibronectin which occur in connective tissues as well as in plasma, or that cleavage products of tissue structural glycoproteins occur in plasma which cross-react with anti-plasma fibronectin.