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胚胎肌腱中胶原蛋白的一种运输形式:氨基末端延伸的电子显微镜证明及分子中存在胱氨酸的证据(鸡胚 - 原胶原蛋白 - 凝胶过滤)

A transport form of collagen from embryonic tendon: electron microscopic demonstration of an NH 2 -terminal extension and evidence suggesting the presence of cystine in the molecule (chick embryo-tropocollagen-gel filtration).

作者信息

Dehm P, Jimenez S A, Olsen B R, Prockop D J

出版信息

Proc Natl Acad Sci U S A. 1972 Jan;69(1):60-4. doi: 10.1073/pnas.69.1.60.

Abstract

When cells were isolated from chickembryo tendons and incubated in vitro for 2-6 hr, essentially all the newly-synthesized collagen was recovered from the incubation medium as a transport form larger than tropocollagen. Experiments in which cells were incubated with [(14)C]cystine suggested that the transport form contained cystine and that it was, in part, stabilized by disulfide bonds. Electron microscopy of segment-long-spacing aggregates prepared from the transport form of collagen showed that the native molecule differed from tropocollagen in that it had an extension of about 13 nm (130 A) at the NH(2)-terminal end.

摘要

当从鸡胚胎肌腱中分离出细胞并在体外培养2 - 6小时时,基本上所有新合成的胶原蛋白都以一种比原胶原蛋白更大的运输形式从培养液中回收。用[¹⁴C]胱氨酸培养细胞的实验表明,这种运输形式含有胱氨酸,并且部分通过二硫键得以稳定。对由胶原蛋白运输形式制备的片段长间距聚集体进行电子显微镜观察显示,天然分子与原胶原蛋白的不同之处在于,它在NH₂末端有一个约13纳米(130埃)的延伸。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a8df/427544/2dc9862accd5/pnas00127-0069-a.jpg

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