对从牛项韧带中酶法纯化得到的弹性蛋白进行X射线分析。

X-ray analysis of enzymically purified elastin from bovine ligamentum nuchae.

作者信息

Serafini-Fracassini A, Field J M

出版信息

Adv Exp Med Biol. 1977;79:679-83. doi: 10.1007/978-1-4684-9093-0_58.

PMID:194469

Abstract

Insoluble elastin has been isolated from bovine ligamentum nuchae by treatment with quanidine and dithiothreitol followed by digestion with collagenase, purified by affinity chromatography. The preparation was subjected to both wide- and low-angle X-ray analysis. The wide-angle diffraction patterns of relaxed and stretched specimens showed only two broad diffraction rings, corresponding to spacings of 4.5 and 9.3 A. No significant reflections were visible in the low-angle diffraction pattern of unstretched specimens, but on stretching an equatorial reflection was produced, corresponding to spacings of between 45 and 50 A.

摘要

通过用胍和二硫苏糖醇处理，随后用胶原酶消化，从牛项韧带中分离出不溶性弹性蛋白，并通过亲和色谱法进行纯化。对该制剂进行了广角和小角X射线分析。松弛和拉伸标本的广角衍射图谱仅显示两个宽衍射环，对应于4.5和9.3 Å的间距。未拉伸标本的小角衍射图谱中没有明显的反射，但在拉伸时会产生一个赤道反射，对应于45至50 Å之间的间距。