从牛胎盘中提取的富含半胱氨酸的胶原蛋白。其组成多肽链的分离及非变性蛋白的一些性质。

R. Jander, J. Rauterberg, B. Voss, D. von Bassewitz
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引用次数: 62

摘要

从牛胎盘的子宫内膜绒毛中分离出一种高分子量的胶原蛋白,经胃蛋白酶有限消化;它类似于Chung等人从人类主动脉中分离出的蛋白质[Chung, E., Rhodes, R. K. and Miller, E. J. (1976) Biochem]。Biophys。Furuto, D. K. and Miller, E. J. (1980) J. Biol。化学学报,1999,19(2):1 - 8。二硫化桥经过变性和还原裂解后,释放出Mr为400000 ~ 55000的3条链。其中两条链可以通过离子交换色谱分离;第三链在非变性条件下聚集,可以在变性和非变性缓冲液中通过顺序分子筛色谱分离。它们的氨基酸组成与基底膜胶原相似,全糖基化羟赖氨酸含量高,但羟脯氨酸含量相对较低,半胱氨酸、酪氨酸和氨基葡萄糖含量高。相对较低的甘氨酸含量表明非胶原结构区域。非变性条件下的还原和另一种胃蛋白酶处理去除了主要含有疏水性氨基酸残基的非胶原区域。通过这种处理,组分的变性温度大大降低,表明天然分子中的二硫桥稳定了三螺旋结构。纤维聚集体被ATP沉淀,在电子显微镜下显示出不同于从其他胶原类型中获得的片段长间距晶体的典型交叉条纹模式。免疫荧光试验显示,该蛋白存在于肾髓质的血管和间质区,但不存在于肾小球和肾小管的基底膜。
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A cysteine-rich collagenous protein from bovine placenta. Isolation of its constituent polypeptide chains and some properties of the non-denatured protein.
A high-molecular-weight collagenous protein was isolated, after limited pepsin digestion, from the endometrial villi of bovine placenta; it resembled the protein isolated from human aortas by Chung et al. [Chung, E., Rhodes, R. K. and Miller, E. J. (1976) Biochem. Biophys. Res. Commun. 71, 1167–1174] and from human placenta by Furuto and Miller [Furuto, D. K. and Miller, E. J. (1980) J. Biol. Chem. 255, 290–295]. After denaturation and reductive cleavage of disulfide bridges three chains with Mr of 40000–55000 were liberated. Two of the chains could be separated by ion-exchange chromatography; the third chain aggregated under non-denaturing conditions and could be isolated by sequential molecular-sieve chromatography in denaturing and non-denaturing buffers. Their amino acid composition resembled that of basement membrane collagens with respect to the high content of completely glycosylated hydroxylysine but differed with respect to their relatively low hydroxyproline content and high values of cysteine, tyrosine and glucosamine. A relatively low glycine content indicated regions of non-collagenous structure. Reduction under non-denaturing conditions and another pepsin treatment removed non-collagenous regions containing mainly hydrophobic amino acid residues. The denaturation temperature of the component was considerably reduced by this treatment, indicating stabilization of triple-helical structures by disulfide bridges in the native molecule. Fibrillar aggregates were precipitated with ATP which showed in the electron microscope a typical crossstriation pattern different to those of segment-long-spacing crystallites obtained from other collagen types. Immunofluorescence tests demonstrated the protein in blood vessels and interstitial areas of the renal medulla but not in basement membranes of glomeruli and tubuli.
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