用环磷酸腺苷和人卵泡液处理后人类精子细胞膜蛋白质构象的变化

Changes in the protein conformation of human spermatozoal membranes after treatment with cyclic adenosine 3':5'-monophosphate and human follicular fluid.

作者信息

Delgado N M, Huacuja L, Pancardo R M, Merchant H, Rosado A

出版信息

Fertil Steril. 1976 Apr;27(4):413-20. doi: 10.1016/s0015-0282(16)41779-6.

Abstract

Infrared spectra in the amide I and amide II regions of acrosomal membranes isolated from ejaculated human spermatozoa indicate the presence of a high proportion of the constitutive proteins in the most stable protein configuration, the antiparallel beta-conformation. Since the infrared spectra obtained with the membranes suspended in D2O or after extraction of the lipid components do not show any significant change, it can be postulated that the antiparallel pleated sheet conformation of human spermatozoal membrane proteins is independent of the hydrated state and of the lipid constitution of the membrane.

摘要

从射出的人类精子中分离出的顶体膜在酰胺I和酰胺II区域的红外光谱表明，大多数组成蛋白以最稳定的蛋白质构型即反平行β-构象存在。由于悬浮在重水中的膜或脂质成分提取后的膜所获得的红外光谱没有显示出任何显著变化，因此可以推测，人类精子膜蛋白的反平行褶皱片层构象与膜的水合状态和脂质组成无关。