Jauregui-Adell J, Pechere J F, Briand G, Richet C, Demaille J G
Eur J Biochem. 1982 Apr 1;123(2):337-45. doi: 10.1111/j.1432-1033.1982.tb19773.x.
The primary structure of the most basic (pI = 4.88) of the two major parvalbumins from frog skeletal muscle (Rana esculenta) has been determined by partial automatic sequencing of the protein which exhibits a free N terminus, and a study of overlapping peptides obtained by cyanogen bromide cleavage and digestion with trypsin, thermolysin and Armillaria mellea protease. This protein shows the typical structure of an alpha-parvalbumin. Comparison of the primary structure of ion-binding loops of alpha and beta-parvalbumins does not provide a clear-cut explanation of their differences in ion-binding properties.
通过对具有游离N端的蛋白质进行部分自动测序，以及对经溴化氰裂解、胰蛋白酶、嗜热菌蛋白酶和蜜环菌蛋白酶消化得到的重叠肽段进行研究，确定了来自青蛙骨骼肌（食用蛙）的两种主要小清蛋白中最基本的一种（pI = 4.88）的一级结构。该蛋白质呈现出α-小清蛋白的典型结构。α-和β-小清蛋白离子结合环的一级结构比较，并未对它们离子结合特性的差异给出明确解释。
