Tamburro A M, Guantieri V, Daga-Gordini D, Abatangelo G
J Biol Chem. 1978 May 10;253(9):2893-4.
Circular dichroism measurements on aqueous solutions of alpha-elastin have given evidence of beta-bend structure at elevated concentrations. When Ca2+ was added, the concentration-dependent conformational transition was somewhat inhibited and the binding of the metal ion was shown, by means of equilibrium dialysis, to be essentially independent from alpha-elastin concentration in the range of 1 to 10 mg/ml. The results obtained are discussed in connection with the elasticity and calcification of elastin.
对α-弹性蛋白水溶液进行的圆二色性测量表明，在高浓度下存在β-转角结构。加入Ca2+后，浓度依赖性构象转变受到一定程度的抑制，并且通过平衡透析表明，在1至10mg/ml的范围内，金属离子的结合基本上与α-弹性蛋白浓度无关。结合弹性蛋白的弹性和钙化对所得结果进行了讨论。
