Cavé A, Saint-Yves A, Parello J, Swärd M, Thulin E, Lindman B
Mol Cell Biochem. 1982 May 14;44(3):161-72. doi: 10.1007/BF00238504.
The inspection of several muscular parvalbumins from different species by two NMR methods (113Cd resonance and 1H relaxation measurements) allows two classes of parvalbumins to be distinguished according to their ion-binding properties. This result is in agreement with the phylogenetic classification of parvalbumins in two series, alpha and beta, which was established on the basis of the primary structures of these proteins. All parvalbumins are characterized by the presence of two primary cationic sites CD and EF, with structural features closely related to those already known on the basis of X-ray crystallographic studies of the beta parvalbumin pI 4.25 from carp muscle. However, parvalbumins of the beta series are characterized by a secondary cation (Ca2+, Mg2+ and other cations) binding site which is absent (or at least inaccessible) in parvalbumins of the alpha series. The major component from thornback ray (pI 4.45) behaves as an alpha parvalbumin as shown by the present NMR studies, although its primary structure suggests a closer similarity with the parvalbumins of the beta series.
通过两种核磁共振方法（¹¹³Cd 共振和¹H 弛豫测量）对来自不同物种的几种肌肉小清蛋白进行检测，可根据其离子结合特性区分出两类小清蛋白。这一结果与基于这些蛋白质一级结构建立的小清蛋白在α和β两个系列中的系统发育分类一致。所有小清蛋白的特征是存在两个主要阳离子位点 CD 和 EF，其结构特征与基于鲤鱼肌肉β小清蛋白 pI 4.25 的 X 射线晶体学研究已知的特征密切相关。然而，β系列小清蛋白的特征是具有一个二级阳离子（Ca²⁺、Mg²⁺和其他阳离子）结合位点，而α系列小清蛋白中不存在（或至少无法接近）该位点。本核磁共振研究表明，棘背鳐的主要成分（pI 4.45）表现为α小清蛋白，尽管其一级结构表明与β系列小清蛋白有更密切的相似性。
